ID ALR2_SALTY Reviewed; 356 AA. AC P06191; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 28-JAN-2026, entry version 156. DE RecName: Full=Alanine racemase, catabolic; DE EC=5.1.1.1; GN Name=dadX; Synonyms=dadB; OrderedLocusNames=STM1802; OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Salmonella. OX NCBI_TaxID=99287; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-25, FUNCTION, RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT. RX PubMed=6391537; DOI=10.1021/bi00317a015; RA Wasserman S.A., Daub E., Grisafi P., Botstein D., Walsh C.T.; RT "Catabolic alanine racemase from Salmonella typhimurium: DNA sequence, RT enzyme purification, and characterization."; RL Biochemistry 23:5182-5187(1984). 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). RN [3] RP PROTEIN SEQUENCE OF 30-44, COFACTOR, AND ACTIVITY REGULATION. RX PubMed=6439236; DOI=10.1021/bi00317a016; RA Badet B., Roise D., Walsh C.T.; RT "Inactivation of the dadB Salmonella typhimurium alanine racemase by D and RT L isomers of beta-substituted alanines: kinetics, stoichiometry, active RT site peptide sequencing, and reaction mechanism."; RL Biochemistry 23:5188-5194(1984). CC -!- FUNCTION: Isomerizes L-alanine to D-alanine which is then oxidized to CC pyruvate by DadA. {ECO:0000269|PubMed:6391537}. 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 Evidence={ECO:0000269|PubMed:6391537}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000269|PubMed:6391537, ECO:0000269|PubMed:6439236}; CC -!- ACTIVITY REGULATION: Inactivated by D- and L-beta-fluoroalanine, D- and CC L-beta-chloroalanine, and O-acetyl-D-serine. CC {ECO:0000269|PubMed:6439236}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=2.1 mM for D-alanine {ECO:0000269|PubMed:6391537}; CC KM=8.2 mM for L-alanine {ECO:0000269|PubMed:6391537}; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:6391537}. CC -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; K02119; AAA27054.1; -; Genomic_DNA. DR EMBL; AE006468; AAL20717.1; -; Genomic_DNA. DR PIR; A29519; A29519. DR RefSeq; NP_460758.1; NC_003197.2. DR RefSeq; WP_000197903.1; NC_003197.2. DR AlphaFoldDB; P06191; -. DR SMR; P06191; -. DR STRING; 99287.STM1802; -. DR PaxDb; 99287-STM1802; -. DR GeneID; 1253321; -. DR KEGG; stm:STM1802; -. DR PATRIC; fig|99287.12.peg.1901; -. DR HOGENOM; CLU_028393_1_0_6; -. DR OMA; HMTHFSD; -. DR PhylomeDB; P06191; -. DR BioCyc; SENT99287:STM1802-MONOMER; -. DR SABIO-RK; P06191; -. DR Proteomes; UP000001014; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008784; F:alanine racemase activity; IBA:GO_Central. DR GO; GO:0042803; F:protein homodimerization activity; IEA:UniProtKB-ARBA. DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central. DR GO; GO:0030632; P:D-alanine biosynthetic process; IBA:GO_Central. DR CDD; cd06827; PLPDE_III_AR_proteobact; 1. DR FunFam; 2.40.37.10:FF:000002; Alanine racemase; 1. DR FunFam; 3.20.20.10:FF:000002; Alanine racemase; 1. DR Gene3D; 3.20.20.10; Alanine racemase; 1. DR Gene3D; 2.40.37.10; Lyase, Ornithine Decarboxylase, Chain A, domain 1; 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 NCBIfam; TIGR00492; alr; 1. DR NCBIfam; NF002970; PRK03646.1; 1. DR PANTHER; PTHR30511; ALANINE RACEMASE; 1. DR PANTHER; PTHR30511:SF0; ALANINE RACEMASE, CATABOLIC-RELATED; 1. 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; Alanine racemase C-terminal domain-like; 1. DR SUPFAM; SSF51419; PLP-binding barrel; 1. DR PROSITE; PS00395; ALANINE_RACEMASE; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Isomerase; Pyridoxal phosphate; KW Reference proteome. FT CHAIN 1..356 FT /note="Alanine racemase, catabolic" FT /id="PRO_0000114561" 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" SQ SEQUENCE 356 AA; 38804 MW; 43DF23205EF25C69 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 YELLCAVAPR VPFVTT //