GenomeNet

Database: UniProt/SWISS-PROT
Entry: ALR1_SALTY
LinkDB: ALR1_SALTY
Original site: 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   28-FEB-2018, entry version 87.
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
RT   and 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.,
RA   Waterston R., Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium
RT   LT2.";
RL   Nature 413:852-856(2001).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-9 AND 29-46, FUNCTION, CATALYTIC ACTIVITY,
RP   COFACTOR, 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
RT   and 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-
CC       alanine. Provides the D-alanine required for cell wall
CC       biosynthesis. {ECO:0000269|PubMed:3524677}.
CC   -!- CATALYTIC ACTIVITY: L-alanine = D-alanine.
CC       {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-
CC       alanine 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}.
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   ProteinModelPortal; P0A1A3; -.
DR   SMR; P0A1A3; -.
DR   STRING; 99287.STM4247; -.
DR   PaxDb; P0A1A3; -.
DR   PRIDE; P0A1A3; -.
DR   EnsemblBacteria; AAL23071; AAL23071; STM4247.
DR   GeneID; 1255773; -.
DR   KEGG; stm:STM4247; -.
DR   PATRIC; fig|99287.12.peg.4467; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031446; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   PhylomeDB; P0A1A3; -.
DR   BioCyc; SENT99287:G1FZD-4289-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
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; -; 2.
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; Complete proteome;
KW   Direct protein sequencing; Isomerase; Peptidoglycan synthesis;
KW   Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    359       Alanine racemase, biosynthetic.
FT                                /FTId=PRO_0000114559.
FT   ACT_SITE     34     34       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000250}.
FT   ACT_SITE    255    255       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000250}.
FT   BINDING     129    129       Substrate. {ECO:0000250}.
FT   BINDING     303    303       Substrate; via amide nitrogen.
FT                                {ECO:0000250}.
FT   MOD_RES      34     34       N6-(pyridoxal phosphate)lysine.
FT   CONFLICT      5      5       T -> S (in Ref. 3; AA sequence).
FT                                {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
//
DBGET integrated database retrieval system