ALR1_SALTY
ID ALR1_SALTY Reviewed; 359 AA.
AC P0A1A3; P06655;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Alanine racemase, biosynthetic;
DE EC=5.1.1.1;
GN Name=alr; OrderedLocusNames=STM4247;
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].
RX PubMed=3524676; DOI=10.1021/bi00359a026;
RA Galakatos N.G., Daub E., Botstein D., Walsh C.T.;
RT "Biosynthetic alr alanine racemase from Salmonella typhimurium: DNA and
RT protein sequence determination.";
RL Biochemistry 25:3255-3260(1986).
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 1-9 AND 29-46, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND SUBUNIT.
RX PubMed=3524677; DOI=10.1021/bi00359a027;
RA Esaki N., Walsh C.T.;
RT "Biosynthetic alanine racemase of Salmonella typhimurium: purification and
RT characterization of the enzyme encoded by the alr gene.";
RL Biochemistry 25:3261-3267(1986).
CC -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine.
CC Provides the D-alanine required for cell wall biosynthesis.
CC {ECO:0000269|PubMed:3524677}.
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:3524677};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:3524677};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:3524677};
CC -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC from L-alanine: step 1/1. {ECO:0000269|PubMed:3524677}.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000269|PubMed:3524677}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:3524677}.
CC -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000305}.
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DR EMBL; M12847; AAA27022.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL23071.1; -; Genomic_DNA.
DR PIR; A24102; A24102.
DR RefSeq; NP_463112.1; NC_003197.2.
DR RefSeq; WP_001147297.1; NC_003197.2.
DR AlphaFoldDB; P0A1A3; -.
DR SMR; P0A1A3; -.
DR STRING; 99287.STM4247; -.
DR PaxDb; P0A1A3; -.
DR EnsemblBacteria; AAL23071; AAL23071; STM4247.
DR GeneID; 1255773; -.
DR KEGG; stm:STM4247; -.
DR PATRIC; fig|99287.12.peg.4467; -.
DR HOGENOM; CLU_028393_1_0_6; -.
DR OMA; WEILCGF; -.
DR PhylomeDB; P0A1A3; -.
DR BioCyc; SENT99287:STM4247-MON; -.
DR UniPathway; UPA00042; UER00497.
DR UniPathway; UPA00219; -.
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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0030632; P:D-alanine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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 Cell shape; Cell wall biogenesis/degradation; Direct protein sequencing;
KW Isomerase; Peptidoglycan synthesis; Pyridoxal phosphate;
KW Reference proteome.
FT CHAIN 1..359
FT /note="Alanine racemase, biosynthetic"
FT /id="PRO_0000114559"
FT ACT_SITE 34
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000250"
FT ACT_SITE 255
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 34
FT /note="N6-(pyridoxal phosphate)lysine"
FT CONFLICT 5
FT /note="T -> S (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 39076 MW; B6527AED8263D65B CRC64;
MQAATVVINR RALRHNLQRL RELAPASKLV AVVKANAYGH GLLETARTLP DADAFGVARL
EEALRLRAGG ITQPILLLEG FFDAADLPTI SAQCLHTAVH NQEQLAALEA VELAEPVTVW
MKLDTGMHRL GVRPEEAEAF YQRLTHCKNV RQPVNIVSHF ARADEPECGA TEHQLDIFNA
FCQGKPGQRS IAASGGILLW PQSHFDWARP GIILYGVSPL EHKPWGPDFG FQPVMSLTSS
LIAVRDHKAG EPVGYGGTWV SERDTRLGVV AMGYGDGYPR AAPSGTPVLV NGREVPIVGR
VAMDMICVDL GPNAQDNAGD PVVLWGEGLP VERIAEMTKV SAYELITRLT SRVAMKYID
