ID   ALR_LACLM               Reviewed;         367 AA.
AC   Q9RLU5; A2RLV4;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 2.
DT   03-AUG-2022, entry version 113.
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=llmg_1704;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10385325; DOI=10.1038/9902;
RA   Hols P., Kleerebezem M., Schank A.N., Ferain T., Hugenholtz J., Delcour J.,
RA   De Vos W.M.;
RT   "Conversion of Lactococcus lactis from homolactic to homoalanine
RT   fermentation through metabolic engineering.";
RL   Nat. Biotechnol. 17:588-592(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
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   -!- BIOTECHNOLOGY: Homoalanine fermentation combined with the disruption of
CC       the alr gene allowed the industrial and stereospecific production
CC       (>99%) of L-alanine, which is used as a food sweetener and for
CC       pharmaceutical applications.
CC   -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
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DR   EMBL; Y18148; CAB56755.2; -; Genomic_DNA.
DR   EMBL; AM406671; CAL98277.1; -; Genomic_DNA.
DR   RefSeq; WP_011835506.1; NZ_WJVF01000040.1.
DR   AlphaFoldDB; Q9RLU5; -.
DR   SMR; Q9RLU5; -.
DR   STRING; 416870.llmg_1704; -.
DR   EnsemblBacteria; CAL98277; CAL98277; llmg_1704.
DR   KEGG; llm:llmg_1704; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_2_1_9; -.
DR   OMA; WEILCGF; -.
DR   PhylomeDB; Q9RLU5; -.
DR   BioCyc; LLAC416870:LLMG_RS08570-MON; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000364; 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   1: Evidence at protein level;
KW   Isomerase; Pyridoxal phosphate.
FT   CHAIN           1..367
FT                   /note="Alanine racemase"
FT                   /id="PRO_0000114527"
FT   ACT_SITE        40
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   ACT_SITE        263
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   BINDING         310
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   MOD_RES         40
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
SQ   SEQUENCE   367 AA;  40677 MW;  B6DE1496315FA814 CRC64;
     MKTSPHRNTS AIVDLKAIRN NIEKFKKHIN PNAEIWPAVK ADAYGHGSIE VSKAVSDLVG
     GFCVSNLDEA IELRNHLVTK PILVLSGIVP EDVDIAAALN ISLTAPSLEW LKLVVQEEAE
     LSDLKIHIGV DSGMGRIGIR DVEEANQMIE LADKYAINFE GIFTHFATAD MADETKFKNQ
     QARFNKIMAG LSRQPKFIHS TNTAAALWHK EQVQAIERLG ISMYGLNPSG KTLELPFEIE
     PALSLVSELT HIKKIAAGET VGYGATYETS EETWIGTVPI GYADGWTRQM QGFKVLVDGK
     FCEIVGRVCM DQMMIKLDKS YPLGTKVTLI GRDKANEITT TDVADWRGTI NYEVLCLLSD
     RIKRIYK