ID   ALR2_SALTI              Reviewed;         356 AA.
AC   Q8Z688;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Alanine racemase, catabolic;
DE            EC=5.1.1.1;
GN   Name=dadX; Synonyms=dadB; OrderedLocusNames=STY1930, t1075;
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: Isomerizes L-alanine to D-alanine which is then oxidized to
CC       pyruvate by DadA. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC         ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000305}.
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DR   EMBL; AL513382; CAD05485.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO68741.1; -; Genomic_DNA.
DR   RefSeq; NP_456309.1; NC_003198.1.
DR   RefSeq; WP_000197904.1; NZ_WSUR01000004.1.
DR   AlphaFoldDB; Q8Z688; -.
DR   SMR; Q8Z688; -.
DR   STRING; 220341.16502989; -.
DR   EnsemblBacteria; AAO68741; AAO68741; t1075.
DR   KEGG; stt:t1075; -.
DR   KEGG; sty:STY1930; -.
DR   PATRIC; fig|220341.7.peg.1947; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_1_0_6; -.
DR   OMA; ELMAVQH; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006522; P:alanine metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 1.
DR   HAMAP; MF_01201; Ala_racemase; 1.
DR   InterPro; IPR000821; Ala_racemase.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR011079; Ala_racemase_C.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR020622; Ala_racemase_pyridoxalP-BS.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   PRINTS; PR00992; ALARACEMASE.
DR   SMART; SM01005; Ala_racemase_C; 1.
DR   SUPFAM; SSF50621; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR00492; alr; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Isomerase; Pyridoxal phosphate.
FT   CHAIN           1..356
FT                   /note="Alanine racemase, catabolic"
FT                   /id="PRO_0000114560"
FT   ACT_SITE        35
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        253
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         301
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         35
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   356 AA;  38732 MW;  43DF23205EF25EE3 CRC64;
     MTRPIQASLD LQVMKQNLAI VRRAAPEARV WSVVKANAYG HGIERVWSAL GATDGFAMLN
     LEEAITLRER GWKGPILMLE GFFHAQDLEA YDTYRLTTCI HSNWQLKALQ NARLNAPLDI
     YVKVNSGMNR LGFQPERAQT VWQQLRAMRN VGEMTLMSHF AQADHPEGIG EAMRRIALAT
     EGLQCAYSLS NSAATLWHPQ AHYDWVRPGI ILYGASPSGQ WRDIADTGLK PVMTLSSEII
     GVQTLSAGER VGYGGGYSVT QEQRIGIVAA GYADGYPRHA PTGTPVLVDG IRTRTVGTVS
     MDMLAVDLTP CPQAGIGTPV ELWGKEIKVD DVASAAGTLG YGLLCAVAPR VPFVTT