ALR2_SALTY
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 03-AUG-2022, entry version 141.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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}.
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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; P06191; -.
DR EnsemblBacteria; AAL20717; AAL20717; 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-MON; -.
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:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0030632; P:D-alanine biosynthetic process; IBA:GO_Central.
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 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
