ID   DCOA_SALTY              Reviewed;         591 AA.
AC   Q03030;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Oxaloacetate decarboxylase alpha chain;
DE            EC=7.2.4.2;
GN   Name=oadA1; Synonyms=oadA; OrderedLocusNames=STM0055;
GN   and
GN   Name=oadA2; OrderedLocusNames=STM3352;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RX   PubMed=1331067; DOI=10.1016/s0021-9258(18)50017-x;
RA   Woehlke G., Wifling K., Dimroth P.;
RT   "Sequence of the sodium ion pump oxaloacetate decarboxylase from Salmonella
RT   typhimurium.";
RL   J. Biol. Chem. 267:22798-22803(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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; M96434; AAA02973.1; -; Unassigned_DNA.
DR   EMBL; AE006468; AAL19019.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL22221.1; -; Genomic_DNA.
DR   PIR; B44465; B44465.
DR   RefSeq; NP_459060.1; NC_003197.2.
DR   RefSeq; NP_462262.1; NC_003197.2.
DR   RefSeq; WP_000150421.1; NC_003197.2.
DR   AlphaFoldDB; Q03030; -.
DR   SMR; Q03030; -.
DR   STRING; 99287.STM0055; -.
DR   TCDB; 3.B.1.1.1; the na(+)-transporting carboxylic acid decarboxylase (nat-dc) family.
DR   PaxDb; Q03030; -.
DR   EnsemblBacteria; AAL19019; AAL19019; STM0055.
DR   EnsemblBacteria; AAL22221; AAL22221; STM3352.
DR   GeneID; 1251573; -.
DR   GeneID; 1254875; -.
DR   KEGG; stm:STM0055; -.
DR   KEGG; stm:STM3352; -.
DR   PATRIC; fig|99287.12.peg.3553; -.
DR   HOGENOM; CLU_000395_4_3_6; -.
DR   OMA; ELHLHCH; -.
DR   PhylomeDB; Q03030; -.
DR   BioCyc; SENT99287:STM3352-MON; -.
DR   Proteomes; UP000001014; 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; Reference proteome; Sodium; Sodium transport;
KW   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_0000146834"
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;  63207 MW;  EE9CF9191E71D6BE CRC64;
     MTIAITDVVL RDAHQSLFAT RLRLDDMLPI AAALDDVGYG SLECWGGATF DACIRFLGED
     PWLRLRELKK AMPKTPLQML LRGQNLLGYR HYADDVVERF VERAVKNGMD VFRVFDAMND
     PRNMKAALQA VRSHGAHAQG TLSYTTSPAH TLQTWLDLTE QLLETGVDSI AIKDMSGILT
     PMAAYELVSE IKKRFEVRLH LHCHATTGMA EMALLKAIEA GVDGVDTAIS SMSATYGHPA
     TEALVATLAG TEHDTGLDIL KLENIAAYFR EVRKKYHAFE GQLKGYDSRI LVAQVPGGML
     TNLESQLKQQ NAADKLDQVL AEIPRVREDL GFIPLVTPTS QIVGTQAVLN VLTGERYKTI
     AKETAGILKG EYGHTPVPVN AALQARVLEG GAPVTCRPAD LLKPELAELE ADVRRQAQEK
     GITLAGNAID DVLTVALFPQ IGLKFLENRN NPAAFEPLPQ AEAAQPVAKA EKPAASGIYT
     VEVEGKAFVV KVSDGGDISQ LTAAVPAASS APVQAAAPAG AGTPVTAPLA GNIWKVIATE
     GQTVAEGDVL LILEAMKMET EIRAAQAGTV RGIAVKSGDA VSVGDTLMTL A