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Database: UniProt
Entry: Q9CH94
LinkDB: Q9CH94
Original site: Q9CH94 
ID   ALR_LACLA               Reviewed;         367 AA.
AC   Q9CH94;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   05-DEC-2018, entry version 105.
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; Synonyms=dal; OrderedLocusNames=LL0844; ORFNames=L0103;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus
OS   lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.GR-1697R;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K.,
RA   Weissenbach J., Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
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   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01201}.
DR   EMBL; AE005176; AAK04942.1; -; Genomic_DNA.
DR   PIR; D86730; D86730.
DR   RefSeq; NP_267000.1; NC_002662.1.
DR   RefSeq; WP_003132601.1; NC_002662.1.
DR   ProteinModelPortal; Q9CH94; -.
DR   SMR; Q9CH94; -.
DR   STRING; 272623.L0103; -.
DR   PaxDb; Q9CH94; -.
DR   EnsemblBacteria; AAK04942; AAK04942; L0103.
DR   GeneID; 1114472; -.
DR   KEGG; lla:L0103; -.
DR   PATRIC; fig|272623.7.peg.903; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   BioCyc; LLAC272623:L0103-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000002196; 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   Complete proteome; Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    367       Alanine racemase.
FT                                /FTId=PRO_0000114526.
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;  40689 MW;  83E5F6F558F3627B CRC64;
     MKTSPHRNTS AIVDLKAIRN NIEKFKKHIH PNAEIWPAVK ADAYGHGSVE VSKAVSDLVG
     GFCVSNLDEA IELRNHLVTK PILVLSGIVP EDVDIAAALN ISLTAPSLEW LKLVVQEEAE
     LSDLKIHIGV DSGMGRIGIR DVEEANQMIE LADKYAINFE GIFTHFATAD MADDTKFKDQ
     QARFNKIMAG LSRKPKFVHS TNTAAALWHK EQVQAIERLG ISMYGLNPSG KTLELPFEIE
     PALSLVSELT HIKKIAAGET VGYGATYETS EETWIGTVPI GYADGWTRQM QGFKVLVNGE
     FCEIVGRVCM DQMMIKLDKS YPLGTKVTLI GRDKTNEITT TDVADWRGTI NYEVLCLLSD
     RIKRIYK
//
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