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Database: UniProt
Entry: A0Q5X2
LinkDB: A0Q5X2
Original site: A0Q5X2 
ID   ALR_FRATN               Reviewed;         365 AA.
AC   A0Q5X2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   16-JAN-2019, entry version 78.
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=FTN_0746;
OS   Francisella tularensis subsp. novicida (strain U112).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=401614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U112;
RX   PubMed=17550600; DOI=10.1186/gb-2007-8-6-r102;
RA   Rohmer L., Fong C., Abmayr S., Wasnick M., Larson Freeman T.J.,
RA   Radey M., Guina T., Svensson K., Hayden H.S., Jacobs M.,
RA   Gallagher L.A., Manoil C., Ernst R.K., Drees B., Buckley D.,
RA   Haugen E., Bovee D., Zhou Y., Chang J., Levy R., Lim R., Gillett W.,
RA   Guenthener D., Kang A., Shaffer S.A., Taylor G., Chen J., Gallis B.,
RA   D'Argenio D.A., Forsman M., Olson M.V., Goodlett D.R., Kaul R.,
RA   Miller S.I., Brittnacher M.J.;
RT   "Comparison of Francisella tularensis genomes reveals evolutionary
RT   events associated with the emergence of human pathogenic strains.";
RL   Genome Biol. 8:R102.1-R102.16(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   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01201}.
DR   EMBL; CP000439; ABK89637.1; -; Genomic_DNA.
DR   RefSeq; WP_003038932.1; NZ_CP009633.1.
DR   ProteinModelPortal; A0Q5X2; -.
DR   SMR; A0Q5X2; -.
DR   PRIDE; A0Q5X2; -.
DR   EnsemblBacteria; ABK89637; ABK89637; FTN_0746.
DR   KEGG; ftn:FTN_0746; -.
DR   KEGG; ftx:AW25_1275; -.
DR   HOGENOM; HOG000263445; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   OrthoDB; 859043at2; -.
DR   BioCyc; FTUL401614:G1G75-778-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000762; 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; 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.
PE   3: Inferred from homology;
KW   Complete proteome; Isomerase; Pyridoxal phosphate.
FT   CHAIN         1    365       Alanine racemase.
FT                                /FTId=PRO_1000138600.
FT   ACT_SITE     32     32       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    257    257       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     128    128       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     305    305       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      32     32       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   365 AA;  41529 MW;  6A0DD20ADF459910 CRC64;
     MNVLEISAQT LRNNIRIIKE YVGSAKICFP VKANAYGHGL ELIVEHSHDL VDFFAVANVL
     EAFRVLDVVE KPVMIFGVIE YNYIDRILSK NIRVSIQDYN DIEKLEKFAK YYNKKPFVHV
     NLNTGMNRMG VDYNDACRTI QRAYESDWLI LEGVYSHLAC ADNRDHPTNI KQKNRFDSIV
     EFTKGLSQDI ICHLSNSYGF LGQKGICYDM VRPGILSYGF LPEFYVDRVI REIKPIARLL
     SKVVKIITLQ EGEGVGYSLI YRGFEGEQLA VIPIGYGDGF PRELGDRGFV NINDVMYPMA
     GRMSMDGLTV SLGINEYDVK VSDTVELISA IPRNRNSAFS IAKQTNTIEY DIMSTLNDRI
     IRKII
//
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