ID   DCOA_SALTI              Reviewed;         591 AA.
AC   Q8XGX8; Q7CBX2;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Oxaloacetate decarboxylase alpha chain;
DE            EC=7.2.4.2;
GN   Name=oadA1; Synonyms=oadA; OrderedLocusNames=STY0064, t0057;
GN   and
GN   Name=oadA2; Synonyms=oadA; OrderedLocusNames=STY3532, t3267;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
CC   -!- FUNCTION: Catalyzes the decarboxylation of oxaloacetate coupled to
CC       Na(+) translocation.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + 2 Na(+)(in) + oxaloacetate = CO2 + 2 Na(+)(out) +
CC         pyruvate; Xref=Rhea:RHEA:57724, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16452, ChEBI:CHEBI:16526, ChEBI:CHEBI:29101; EC=7.2.4.2;
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC   -!- SUBUNIT: Composed of three chains (alpha, beta, and gamma).
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DR   EMBL; AL513382; CAD01210.1; -; Genomic_DNA.
DR   EMBL; AL513382; CAD07867.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO67790.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO70802.1; -; Genomic_DNA.
DR   RefSeq; NP_454666.1; NC_003198.1.
DR   RefSeq; NP_457728.1; NC_003198.1.
DR   RefSeq; WP_000150450.1; NZ_WSUR01000074.1.
DR   AlphaFoldDB; Q8XGX8; -.
DR   SMR; Q8XGX8; -.
DR   STRING; 220341.16501339; -.
DR   PRIDE; Q8XGX8; -.
DR   EnsemblBacteria; AAO67790; AAO67790; t0057.
DR   EnsemblBacteria; AAO70802; AAO70802; t3267.
DR   KEGG; stt:t0057; -.
DR   KEGG; stt:t3267; -.
DR   KEGG; sty:STY0064; -.
DR   KEGG; sty:STY3532; -.
DR   PATRIC; fig|220341.7.peg.3596; -.
DR   eggNOG; COG0511; Bacteria.
DR   eggNOG; COG5016; Bacteria.
DR   HOGENOM; CLU_000395_4_3_6; -.
DR   OMA; ELHLHCH; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0015451; F:decarboxylation-driven active transmembrane transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:InterPro.
DR   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR003379; Carboxylase_cons_dom.
DR   InterPro; IPR005776; OadA.
DR   InterPro; IPR000891; PYR_CT.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   Pfam; PF02436; PYC_OADA; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   TIGRFAMs; TIGR01108; oadA; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
KW   Biotin; Ion transport; Sodium; Sodium transport; Translocase; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..591
FT                   /note="Oxaloacetate decarboxylase alpha chain"
FT                   /id="PRO_0000232701"
FT   DOMAIN          3..263
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT   DOMAIN          518..591
FT                   /note="Biotinyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   MOD_RES         557
FT                   /note="N6-biotinyllysine"
FT                   /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT                   ProRule:PRU01066"
SQ   SEQUENCE   591 AA;  63373 MW;  10F3A3BE94AB7DD2 CRC64;
     MTIAITDVVL RDAHQSLFAT RLRLDDMLPI AAQLDDVGYG SLECWGGATF DACIRFLGED
     PWLRLRELKK AMPKTPLQML LRGQNLLGYR HYADDVVERF VERAVKNGMD VFRVFDAMND
     PRNMKAALQA VRSHGAHAQG TLSYTTSPAH TLQTWLDLTE QLLETGVDSI AIKDMSGILT
     PMAAFELVSE IKKRFEVRLH LHCHATTGMA EMALLKAIEA GVDGVDTAIS SMSATYGHPA
     TEALVATLAG TEHDTGLDIL KLENIAAYFR EVRKKYHAFE GQLKGYDSRI LVAQVPGGML
     TNLESQLKQQ NAADRLDQVL AEIPRVREDL GFIPLVTPTS QIVGTQAVLN VLTGERYKTI
     AKETAGILKG EYGHTPVPVN AALQARVLEG SAPVTCRPAD LLKPELAELE ADVRRQAQEK
     GITLAGNAID DVLTVALFPQ IGLKFLENRH NPAAFEPLPQ AEAAQPVAKA EKPAASGIYT
     VEVEGKAFVV RVSDGGDISQ LTTAVPAASS APVQAAAPAG AGTPVTAPLA GNIWKVIATE
     GQSVAEGDVL LILEAMKMET EIRAAQAGTV RGIAVKSGDA VSVGDTLMTL A