OADC1_PSEPW
ID OADC1_PSEPW Reviewed; 289 AA.
AC B1J195;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Oxaloacetate decarboxylase 1 {ECO:0000255|HAMAP-Rule:MF_01299};
DE EC=4.1.1.112 {ECO:0000255|HAMAP-Rule:MF_01299};
GN OrderedLocusNames=PputW619_1029;
OS Pseudomonas putida (strain W619).
OC Bacteria; Proteobacteria; 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; ACA71534.1; -; Genomic_DNA.
DR RefSeq; WP_012312950.1; NC_010501.1.
DR AlphaFoldDB; B1J195; -.
DR SMR; B1J195; -.
DR STRING; 390235.PputW619_1029; -.
DR PRIDE; B1J195; -.
DR EnsemblBacteria; ACA71534; ACA71534; PputW619_1029.
DR KEGG; ppw:PputW619_1029; -.
DR eggNOG; COG2513; Bacteria.
DR HOGENOM; CLU_027389_3_2_6; -.
DR OMA; IAHACSY; -.
DR OrthoDB; 1485205at2; -.
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..289
FT /note="Oxaloacetate decarboxylase 1"
FT /id="PRO_0000364069"
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; 31450 MW; 73C19FEEC4BD7DEF CRC64;
MPKASHQDLR FAFRELLASG SCYHTASVFD PMSARIAADL GFEVGILGGS VASLQVLAAP
DFALITLSEF VEQATRIGRV AQLPVLADAD HGYGNALNVM RTVIELERAG VAALTIEDTL
LPAQFGRKST DLIPVEEGVG KIRAALEARV DSSLSIIART NAGVLSTEEI IVRTQSYQKA
GADAICMVGV KDFEQLEQIA GHLSVPLMLV TYANPNLHDD ERLARLGVRI VVDGHAAYFA
AIKATYDCLR LQRGQQNKSE NLTATELSHT YTQPEDYIRW AKEYMSVDE
