ID A0A089WN80_9PSED Unreviewed; 289 AA.
AC A0A089WN80;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Oxaloacetate decarboxylase {ECO:0000256|HAMAP-Rule:MF_01299};
DE EC=4.1.1.112 {ECO:0000256|HAMAP-Rule:MF_01299};
GN ORFNames=LK03_01240 {ECO:0000313|EMBL:AIR87942.1};
OS Pseudomonas cremoricolorata.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=157783 {ECO:0000313|EMBL:AIR87942.1, ECO:0000313|Proteomes:UP000029493};
RN [1] {ECO:0000313|EMBL:AIR87942.1, ECO:0000313|Proteomes:UP000029493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND07 {ECO:0000313|EMBL:AIR87942.1,
RC ECO:0000313|Proteomes:UP000029493};
RA Chan K.-G.;
RL Submitted (SEP-2014) 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:0000256|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:0000256|HAMAP-
CC Rule:MF_01299};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01299};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01299};
CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000256|HAMAP-
CC Rule:MF_01299}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase family. Oxaloacetate
CC decarboxylase subfamily. {ECO:0000256|HAMAP-Rule:MF_01299}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Oxaloacetate decarboxylase family. {ECO:0000256|ARBA:ARBA00005838}.
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DR EMBL; CP009455; AIR87942.1; -; Genomic_DNA.
DR RefSeq; WP_038410726.1; NZ_CP009455.1.
DR AlphaFoldDB; A0A089WN80; -.
DR STRING; 157783.LK03_01240; -.
DR KEGG; psw:LK03_01240; -.
DR eggNOG; COG2513; Bacteria.
DR OrthoDB; 9771433at2; -.
DR Proteomes; UP000029493; 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; Phosphoenolpyruvate-binding domains; 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 PANTHER; PTHR42905:SF3; OXALOACETATE DECARBOXYLASE; 1.
DR PANTHER; PTHR42905; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR Pfam; PF13714; PEP_mutase; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW Rule:MF_01299};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01299};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01299};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01299}; Reference proteome {ECO:0000313|Proteomes:UP000029493}.
FT BINDING 50
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01299"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01299"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01299"
FT BINDING 235
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01299"
SQ SEQUENCE 289 AA; 31565 MW; 75F0BDED84409E7C CRC64;
MPKASHHDLR IAFRDLLASQ SCYHTASVFD PMSARIASDL GFEVGILGGS VASLQVLAAP
DFALITLSEF VEQATRIGRV AQLPFLADAD HGYGNALNVM RTVIELERAG VSALTIEDTL
LPAQFGRKST DLISVDEGVG KIRAAIEARV DSAMAIIGRT NAGVLSTEEV IHRTQSYQKA
GADGICMVGI KDFDHLEQIS SHLSVPLMLV SYGNPNLRDD QRLAELGVRI VVDGHAAYFA
AIKATYDCLR LQRGQQNKSE NLSATELSHT YTQPEDYIRW AKEYMNVEE
//
