ID OADC2_PSEPW Reviewed; 302 AA.
AC B1JFP4;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Oxaloacetate decarboxylase 2 {ECO:0000255|HAMAP-Rule:MF_01299};
DE EC=4.1.1.112 {ECO:0000255|HAMAP-Rule:MF_01299};
GN OrderedLocusNames=PputW619_5152;
OS Pseudomonas putida (strain W619).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=390235;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W619;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Taghavi S., Vangronsveld D., van der Lelie D.,
RA Richardson P.;
RT "Complete sequence of Pseudomonas putida W619.";
RL Submitted (FEB-2008) 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; CP000949; ACA75628.1; -; Genomic_DNA.
DR AlphaFoldDB; B1JFP4; -.
DR SMR; B1JFP4; -.
DR STRING; 390235.PputW619_5152; -.
DR KEGG; ppw:PputW619_5152; -.
DR eggNOG; COG2513; Bacteria.
DR HOGENOM; CLU_027389_3_2_6; -.
DR OrthoDB; 9771433at2; -.
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; Lyase; Magnesium; Metal-binding.
FT CHAIN 1..302
FT /note="Oxaloacetate decarboxylase 2"
FT /id="PRO_0000364070"
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 302 AA; 32616 MW; BCBB9B052052DCFB CRC64;
MIERSHHELR KAFGDLLQGH VCKFAASVFD PISVRMASDL GFEVGIQGGS VASLQVLGAP
DIALLTLDEY VEQVTRVGRA SQIPVIADAD HGFGNALNVM RTVSELQKAG VAALTLEDTH
LPARYEEQSP VLIGEEEAAA KIYAARFSRS DDSLSIIART NVAATTLEDS IARTAAYEKA
GADAICLVGV KDFHHLAALT EHLTTPIMLI NYGNPALCDV EKLSAANVRI VVNGHAPYFS
AIKSIYQALR EQSGSQGPEL SLPELISKYT RVESYREWTK TYLKVGHDSP CGVTPRGPQL
CN
//
