ID   OADC_RHOPA              Reviewed;         288 AA.
AC   Q6N509;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=RPA3174;
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=14704707; DOI=10.1038/nbt923;
RA   Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA   Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA   Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA   Harrison F.H., Gibson J., Harwood C.S.;
RT   "Complete genome sequence of the metabolically versatile photosynthetic
RT   bacterium Rhodopseudomonas palustris.";
RL   Nat. Biotechnol. 22:55-61(2004).
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; BX572603; CAE28615.1; -; Genomic_DNA.
DR   RefSeq; WP_011158719.1; NC_005296.1.
DR   AlphaFoldDB; Q6N509; -.
DR   SMR; Q6N509; -.
DR   STRING; 258594.RPA3174; -.
DR   PRIDE; Q6N509; -.
DR   EnsemblBacteria; CAE28615; CAE28615; RPA3174.
DR   GeneID; 66894258; -.
DR   KEGG; rpa:RPA3174; -.
DR   eggNOG; COG2513; Bacteria.
DR   HOGENOM; CLU_027389_3_2_5; -.
DR   OMA; RGEHFLG; -.
DR   PhylomeDB; Q6N509; -.
DR   BioCyc; RPAL258594:TX73_RS16190-MON; -.
DR   Proteomes; UP000001426; 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: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; Reference proteome.
FT   CHAIN           1..288
FT                   /note="Oxaloacetate decarboxylase"
FT                   /id="PRO_0000364075"
FT   BINDING         47
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01299"
FT   BINDING         85
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01299"
FT   BINDING         156
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01299"
FT   BINDING         232
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01299"
SQ   SEQUENCE   288 AA;  30189 MW;  BBF37136E589B772 CRC64;
     MAWRDRRGAL RAILTGSACV RPASVYDAIS IRIADDLGFP FGMFGGSVAS LAILGDPDIA
     LITLTELAEQ VRRMSRAAAL PVVVDADHGY GNALNVRRTV EELEAAGAAG LTIEDTLLPQ
     AYGEAKPQLV SREEGLGKIK AALDARRDPN LVIIGRTGAC SITSLDDAIE RALAYQAAGV
     DALFFTGVKT RAQLEAISAA TTLPIALGSP PAELGDFDHL AERRVRIAVQ GHAPIAAATE
     AVFKTLSAIK DGAAPKALTG LASAELMDKV TRADVVAERG EHFLGVKR