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Database: UniProt
Entry: Q9RLU5
LinkDB: Q9RLU5
Original site: Q9RLU5 
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   05-DEC-2018, entry version 102.
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.
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.,
RA   Delcour J., 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-
CC       alanine. May also act on other amino acids. {ECO:0000255|HAMAP-
CC       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-
CC       alanine from L-alanine: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   -!- BIOTECHNOLOGY: Homoalanine fermentation combined with the
CC       disruption of the alr gene allowed the industrial and
CC       stereospecific production (>99%) of L-alanine, which is used as a
CC       food sweetener and for pharmaceutical applications.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01201}.
DR   EMBL; Y18148; CAB56755.2; -; Genomic_DNA.
DR   EMBL; AM406671; CAL98277.1; -; Genomic_DNA.
DR   RefSeq; WP_011835506.1; NC_009004.1.
DR   ProteinModelPortal; Q9RLU5; -.
DR   SMR; Q9RLU5; -.
DR   STRING; 416870.llmg_1704; -.
DR   EnsemblBacteria; CAL98277; CAL98277; llmg_1704.
DR   KEGG; llm:llmg_1704; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   BioCyc; LLAC416870:LLMG_RS08570-MONOMER; -.
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   Complete proteome; Isomerase; Pyridoxal phosphate.
FT   CHAIN         1    367       Alanine racemase.
FT                                /FTId=PRO_0000114527.
FT   ACT_SITE     40     40       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    263    263       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     136    136       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     310    310       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      40     40       N6-(pyridoxal phosphate)lysine.
FT                                {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
//
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