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Database: UniProt
Entry: Q5NH94
LinkDB: Q5NH94
Original site: Q5NH94 
ID   ALR_FRATT               Reviewed;         365 AA.
AC   Q5NH94;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   05-DEC-2018, entry version 88.
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=FTT_0573;
OS   Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=177416;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCHU S4 / Schu 4;
RX   PubMed=15640799; DOI=10.1038/ng1499;
RA   Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M.,
RA   Fuxelius H.-H., Garcia E., Haelltorp G., Johansson D., Isherwood K.E.,
RA   Karp P.D., Larsson E., Liu Y., Michell S., Prior J., Prior R.,
RA   Malfatti S., Sjoestedt A., Svensson K., Thompson N., Vergez L.,
RA   Wagg J.K., Wren B.W., Lindler L.E., Andersson S.G.E., Forsman M.,
RA   Titball R.W.;
RT   "The complete genome sequence of Francisella tularensis, the causative
RT   agent of tularemia.";
RL   Nat. Genet. 37:153-159(2005).
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; AJ749949; CAG45206.1; -; Genomic_DNA.
DR   RefSeq; WP_003029065.1; NZ_CP010290.1.
DR   RefSeq; YP_169598.1; NC_006570.2.
DR   ProteinModelPortal; Q5NH94; -.
DR   SMR; Q5NH94; -.
DR   IntAct; Q5NH94; 2.
DR   STRING; 177416.FTT_0573; -.
DR   DNASU; 3192353; -.
DR   EnsemblBacteria; CAG45206; CAG45206; FTT_0573.
DR   GeneID; 3192353; -.
DR   KEGG; ftu:FTT_0573; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000263445; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   BioCyc; FTUL177416:G1G1C-660-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000001174; 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; Reference proteome.
FT   CHAIN         1    365       Alanine racemase.
FT                                /FTId=PRO_1000073096.
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;  41491 MW;  A76A5DA5E1CA9273 CRC64;
     MNILKISKQT LRNNIKIIRE YIGNAKMCFP VKANAYGHGI EDIVENTHDL VDFFAVANSL
     EAFRVTAVAK NPVLVFGVIY YEYIEKMISE NIRVSIQDYE DIEKLEQIAK ELDKKVYAHI
     NINTGMNRMG VDYNDACRTI QRAYESDWLI LEGVYSHLAC ADNRDHPTNI KQKNRFDSIV
     KFTKGLSQDI ICHLSNSYGF LGQKGICYDM VRPGILSYGF LPEFYVDRVI REIKPIARLL
     SKVVKIITLQ EGEGVGYSLI YRGFEDEQLA VIPIGYGDGF PRELGDRGFV NINDVMYPMA
     GRMSMDGLTV SLGINEYDVK VGDTVELISA IPRNRNSAFS IAKQTNTIEY DIMSTLNDRI
     IRKII
//
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