ALR_LACPL
ID ALR_LACPL Reviewed; 375 AA.
AC O08445; F9UKZ8;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Alanine racemase {ECO:0000255|HAMAP-Rule:MF_01201};
DE EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN Name=alr; OrderedLocusNames=lp_0523;
OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS (Lactobacillus plantarum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=220668;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=9171436; DOI=10.1128/jb.179.11.3804-3807.1997;
RA Hols P., Defrenne C., Ferain T., Derzelle S., Delplace B., Delcour J.;
RT "The alanine racemase gene is essential for growth of Lactobacillus
RT plantarum.";
RL J. Bacteriol. 179:3804-3807(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA Siezen R.J.;
RT "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=22156394; DOI=10.1128/jb.06275-11;
RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA Kleerebezem M., van Hijum S.A.;
RT "Complete resequencing and reannotation of the Lactobacillus plantarum
RT WCFS1 genome.";
RL J. Bacteriol. 194:195-196(2012).
CC -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May
CC also act on other amino acids. {ECO:0000255|HAMAP-Rule:MF_01201}.
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:0000255|HAMAP-Rule:MF_01201};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC from L-alanine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01201}.
CC -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000255|HAMAP-
CC Rule:MF_01201}.
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DR EMBL; Y08941; CAA70140.1; -; Genomic_DNA.
DR EMBL; AL935263; CCC78013.1; -; Genomic_DNA.
DR RefSeq; WP_003642062.1; NC_004567.2.
DR RefSeq; YP_004888527.1; NC_004567.2.
DR AlphaFoldDB; O08445; -.
DR SMR; O08445; -.
DR STRING; 220668.lp_0523; -.
DR PRIDE; O08445; -.
DR EnsemblBacteria; CCC78013; CCC78013; lp_0523.
DR GeneID; 57024294; -.
DR KEGG; lpl:lp_0523; -.
DR PATRIC; fig|220668.9.peg.431; -.
DR eggNOG; COG0787; Bacteria.
DR HOGENOM; CLU_028393_2_1_9; -.
DR OMA; WEILCGF; -.
DR PhylomeDB; O08445; -.
DR BioCyc; LPLA220668:G1GW0-434-MON; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000000432; 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:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
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; Reference proteome.
FT CHAIN 1..375
FT /note="Alanine racemase"
FT /id="PRO_0000114528"
FT ACT_SITE 41
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT ACT_SITE 270
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 317
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT MOD_RES 41
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
SQ SEQUENCE 375 AA; 40710 MW; 844E9BAC5FF3463B CRC64;
MVVIGEHRHT QVTVDLQAIK TNISNEMAQK DELTELWAVV KANGYGHGII QVAQAAKEAG
ATGFCVAILD EALALRAAGF AEPILVLGIT EPEYAPLVAE KDISLAVGTQ DWLTTAAAIL
AANQVTTPLH VHLALDTGMG RIGFQTPEEL ATAVTTLRQP QSPFDFEGIF THFATADQAD
DTYFTHQLNN WKHLIAVVDE LPRYVHVSNS ATSLWHQACN GNMVRFGVAL YGLNPSGREL
SAPYPLQPAL SLTARLTFVK RLARGKSVSY GATYTAAQDE WIGTVPIGYA DGYERRLQGF
HVLVDGEFCE IVGRVCMDQL MVRLPHEVPV GAKVTLVGTD GARTISLQDI ADYCGTIHYE
IACGLAPRVP RVYID
