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Database: UniProt/SWISS-PROT
Entry: ALR_BURMS
LinkDB: ALR_BURMS
Original site: ALR_BURMS 
ID   ALR_BURMS               Reviewed;         356 AA.
AC   A1V591;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   28-FEB-2018, entry version 72.
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=BMASAVP1_A2078;
OS   Burkholderia mallei (strain SAVP1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320388;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAVP1;
RA   DeShazer D., Woods D.E., Nierman W.C.;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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: L-alanine = D-alanine. {ECO:0000255|HAMAP-
CC       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; CP000526; ABM52249.1; -; Genomic_DNA.
DR   RefSeq; WP_004191260.1; NC_008785.1.
DR   ProteinModelPortal; A1V591; -.
DR   SMR; A1V591; -.
DR   PRIDE; A1V591; -.
DR   EnsemblBacteria; ABM52249; ABM52249; BMASAVP1_A2078.
DR   KEGG; bmv:BMASAVP1_A2078; -.
DR   HOGENOM; HOG000031446; -.
DR   KO; K01775; -.
DR   OMA; WRGPILL; -.
DR   UniPathway; UPA00042; UER00497.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
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   3: Inferred from homology;
KW   Isomerase; Pyridoxal phosphate.
FT   CHAIN         1    356       Alanine racemase.
FT                                /FTId=PRO_1000065977.
FT   ACT_SITE     35     35       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    253    253       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     130    130       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     301    301       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      35     35       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   356 AA;  38334 MW;  B29D6F1F142DD41E CRC64;
     MPRPISATIH TAALANNLSV VRRHAAQSKV WAIVKANAYG HGLARVFPGL RGTDGFGLLD
     LDEAVKLREL GWAGPILLLE GFFRSTDIDV IDRYSLTTAV HNDEQMRMLE TARLSKPVNV
     QLKMNSGMNR LGYTPEKYRA AWERARACPG IGQITLMTHF SDADGERGVA EQMATFERGA
     QGIAGARSFA NSAAVLWHPS AHFDWVRPGI MLYGASPSGR AADIADRGLK PTMTLASELI
     AVQTLAKGQA VGYGSMFVAE DTMRIGVVAC GYADGYPRIA PEGTPVVVDG VRTRIVGRVS
     MDMLTVDLTP VPQAGVGARV ELWGETLPID DVAARCMTVG YELMCAVAPR VPVRAE
//
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