ID W9T704_9PSED Unreviewed; 286 AA.
AC W9T704;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Oxaloacetate decarboxylase {ECO:0000256|HAMAP-Rule:MF_01299};
DE EC=4.1.1.112 {ECO:0000256|HAMAP-Rule:MF_01299};
GN Name=bcpA {ECO:0000313|EMBL:EXF43161.1};
GN ORFNames=BAY1663_04416 {ECO:0000313|EMBL:EXF43161.1};
OS Pseudomonas sp. BAY1663.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1439940 {ECO:0000313|EMBL:EXF43161.1, ECO:0000313|Proteomes:UP000019475};
RN [1] {ECO:0000313|EMBL:EXF43161.1, ECO:0000313|Proteomes:UP000019475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAY1663 {ECO:0000313|EMBL:EXF43161.1,
RC ECO:0000313|Proteomes:UP000019475};
RA Gyula P., Szabo Z., Robotka H., Bihari Z.;
RT "Genome sequencing of Pseudomonas sp. BAY1663.";
RL Submitted (DEC-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXF43161.1}.
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DR EMBL; AZSV01000097; EXF43161.1; -; Genomic_DNA.
DR RefSeq; WP_037044022.1; NZ_AZSV01000097.1.
DR AlphaFoldDB; W9T704; -.
DR STRING; 1439940.BAY1663_04416; -.
DR PATRIC; fig|1439940.3.peg.4377; -.
DR eggNOG; COG2513; Bacteria.
DR OrthoDB; 9771433at2; -.
DR Proteomes; UP000019475; Unassembled WGS sequence.
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}; Pyruvate {ECO:0000313|EMBL:EXF43161.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019475}.
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01299"
FT BINDING 87
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01299"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01299"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01299"
SQ SEQUENCE 286 AA; 31308 MW; 557824B3B0073A60 CRC64;
MRLSHHTLRR NFRQLLSADR CYHTASVFDP MSARIAADLG FEVGILGGSV ASLQVLAAPD
FNLITLSEFV EQATRICRVA QLPVLADADH GYGNALNVMR TVTELERAGI SALTIEDTLL
PPKFGRKSTD LIGMFEAVGK IRAALEARVD PELAIIARTN AGVIGFEEVI ARAQAYEKAG
ADAICLVGIE DFDHLHSIAS QLSTPLMLVT YGNPNLRDNA RLAELGVRIV VNGHAAYFAA
IKATYDCLRE QRQIDALDLN ASQLSVKYST ADEYVVWAEE YMQVKE
//
