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Database: UniProt/TrEMBL
Entry: A0A0F6AU05_BRUA1
LinkDB: A0A0F6AU05_BRUA1
Original site: A0A0F6AU05_BRUA1 
ID   A0A0F6AU05_BRUA1        Unreviewed;       399 AA.
AC   A0A0F6AU05;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-SEP-2017, entry version 18.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   OrderedLocusNames=BAbS19_II02960 {ECO:0000313|EMBL:ACD73807.1};
OS   Brucella abortus (strain S19).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=430066 {ECO:0000313|EMBL:ACD73807.1, ECO:0000313|Proteomes:UP000002565};
RN   [1] {ECO:0000313|EMBL:ACD73807.1, ECO:0000313|Proteomes:UP000002565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S19 {ECO:0000313|EMBL:ACD73807.1,
RC   ECO:0000313|Proteomes:UP000002565};
RX   PubMed=18478107; DOI=10.1371/journal.pone.0002193;
RA   Crasta O.R., Folkerts O., Fei Z., Mane S.P., Evans C.,
RA   Martino-Catt S., Bricker B., Yu G., Du L., Sobral B.W.;
RT   "Genome sequence of Brucella abortus vaccine strain S19 compared to
RT   virulent strains yields candidate virulence genes.";
RL   PLoS ONE 3:E2193-E2193(2008).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY: L-alanine = D-alanine. {ECO:0000256|HAMAP-
CC       Rule:MF_01201, ECO:0000256|SAAS:SAAS00630646}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01201,
CC         ECO:0000256|PIRSR:PIRSR600821-50,
CC         ECO:0000256|SAAS:SAAS00758845};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|SAAS:SAAS00630654}.
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DR   EMBL; CP000888; ACD73807.1; -; Genomic_DNA.
DR   RefSeq; WP_002967219.1; NC_010740.1.
DR   ProteinModelPortal; A0A0F6AU05; -.
DR   STRING; 430066.BAbS19_II02960; -.
DR   EnsemblBacteria; ACD73807; ACD73807; BAbS19_II02960.
DR   GeneID; 29595317; -.
DR   KEGG; bmc:BAbS19_II02960; -.
DR   PATRIC; fig|359391.4.peg.2606; -.
DR   KO; K01775; -.
DR   OMA; WRGPILL; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000002565; Chromosome 2.
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 {ECO:0000313|Proteomes:UP000002565};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456}.
FT   DOMAIN      262    388       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     49     49       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    283    283       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     148    148       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     331    331       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      49     49       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   399 AA;  42727 MW;  C73ADE0206F6B037 CRC64;
     MVEMSLPFSQ DERDLAAGGI LTIDLAALRH NYSAIATRIA PTRTAAVVKA DAYGLGASRV
     APAFYEAGCR DFFVAHLGEA VALKPFLKPD ATLYVLNGLQ PGTEAACARE GILPVLNSLE
     QVENWAALAT RLGKKLPALL QFDTGMSRLG LSAKEFDRLL ENVTLLSRID IKFAISHLAN
     GDEPGNAVNA RQLAKMTALL ARLPKLPAAL ANSGGTFLGK TYYFDLARPG IALYGIDPER
     QHDFSDKVAH ENKKPKHSIL PVLTLSARVI QVRDVDKGAT VGYGGTYVAN GPMRIATIAV
     GYADGLFRSL SNKGAAFFGD TRLPIIGRVS MDSITLDVTS LPEGTLKLGS LVELIGPHQR
     LEDVARDCDT IPYEILTALG NRYARVYVYV NGGGTSTTA
//
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