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Database: UniProt/TrEMBL
Entry: A0A0U5IFY3_9RHIZ
LinkDB: A0A0U5IFY3_9RHIZ
Original site: A0A0U5IFY3_9RHIZ 
ID   A0A0U5IFY3_9RHIZ        Unreviewed;       399 AA.
AC   A0A0U5IFY3;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-SEP-2017, entry version 14.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   Name=alr {ECO:0000313|EMBL:CUW45330.1};
GN   ORFNames=BF3285c2_0450 {ECO:0000313|EMBL:CUW45330.1};
OS   Brucella vulpis.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=981386 {ECO:0000313|EMBL:CUW45330.1};
RN   [1] {ECO:0000313|EMBL:CUW45330.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=F60 {ECO:0000313|EMBL:CUW45330.1};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) 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: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; LN997864; CUW45330.1; -; Genomic_DNA.
DR   RefSeq; WP_059244569.1; NZ_LN998034.1.
DR   EnsemblBacteria; CUW45330; CUW45330; BF3285c2_0450.
DR   KEGG; bvl:BF3285c2_0450; -.
DR   PATRIC; fig|981386.3.peg.2795; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000062743; 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:UP000062743};
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;  42695 MW;  895F8F52A2BD2040 CRC64;
     MVEMSLPFSQ DERDLAAGGI LTIDLAALRH NYSAIATRIA PTRTAAVVKA DAYGLGASRV
     APAFYEAGCR DFFVAHLGEA VALKPFLKPD ATLYVLNGLQ PGTEAACARE GILPVLNSLE
     QVENWAALAT RLGKKLPALL QFDTGMSRLG LSAKEFDRLL ENVTLLSRID IKFAISHLAN
     GDEPGNAANA HQLAKMTALL ARLPKLPAAL ANSGGTFLGK TYYFDLARPG IALYGIDPER
     QHDFSDKVAH ENKEPKHSIL PVLTLSARVI QVRDVDKGAT VGYGGTYVAK GPMRIATIAV
     GYADGLFRSL SNKGAAFFGD TRLPIIGRVS MDSITLDVTS LPEGTLKLGS LVELIGPHQR
     LEDVARDCDT IPYEILTALG NRYARVYVYV NGGGTSTTA
//
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