OADC_PSEA8
ID OADC_PSEA8 Reviewed; 287 AA.
AC B7V1T5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=PLES_52581;
OS Pseudomonas aeruginosa (strain LESB58).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=557722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LESB58;
RX PubMed=19047519; DOI=10.1101/gr.086082.108;
RA Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I.,
RA Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L., Quail M.A.,
RA Lennard N., Bignell A., Clarke L., Seeger K., Saunders D., Harris D.,
RA Parkhill J., Hancock R.E.W., Brinkman F.S.L., Levesque R.C.;
RT "Newly introduced genomic prophage islands are critical determinants of in
RT vivo competitiveness in the Liverpool epidemic strain of Pseudomonas
RT aeruginosa.";
RL Genome Res. 19:12-23(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 family. Oxaloacetate
CC decarboxylase subfamily. {ECO:0000255|HAMAP-Rule:MF_01299}.
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DR EMBL; FM209186; CAW30012.1; -; Genomic_DNA.
DR RefSeq; WP_003121125.1; NC_011770.1.
DR AlphaFoldDB; B7V1T5; -.
DR SMR; B7V1T5; -.
DR KEGG; pag:PLES_52581; -.
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..287
FT /note="Oxaloacetate decarboxylase"
FT /id="PRO_1000140442"
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 287 AA; 31321 MW; 807D13799A49CE0B CRC64;
MHRASHHELR AMFRALLDSS RCYHTASVFD PMSARIAADL GFECGILGGS VASLQVLAAP
DFALITLSEF VEQATRIGRV ARLPVIADAD HGYGNALNVM RTVVELERAG IAALTIEDTL
LPAQFGRKST DLICVEEGVG KIRAALEARV DPALTIIART NAELIDVDAV IQRTLAYQEA
GADGICLVGV RDFAHLEAIA EHLHIPLMLV TYGNPQLRDD ARLARLGVRV VVNGHAAYFA
AIKATYDCLR EERGAVASDL TASELSKKYT FPEEYQAWAR DYMEVKE
