GenomeNet

Database: UniProt
Entry: Q5ZXJ2
LinkDB: Q5ZXJ2
Original site: Q5ZXJ2 
ID   ALR_LEGPH               Reviewed;         357 AA.
AC   Q5ZXJ2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   05-DEC-2018, entry version 92.
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=lpg0739;
OS   Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 /
OS   ATCC 33152 / DSM 7513).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=272624;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX   PubMed=15448271; DOI=10.1126/science.1099776;
RA   Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M.,
RA   Asamani G., Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J.,
RA   Steshenko V., Park S.H., Zhao B., Teplitskaya E., Edwards J.R.,
RA   Pampou S., Georghiou A., Chou I.-C., Iannuccilli W., Ulz M.E.,
RA   Kim D.H., Geringer-Sameth A., Goldsberry C., Morozov P., Fischer S.G.,
RA   Segal G., Qu X., Rzhetsky A., Zhang P., Cayanis E., De Jong P.J.,
RA   Ju J., Kalachikov S., Shuman H.A., Russo J.J.;
RT   "The genomic sequence of the accidental pathogen Legionella
RT   pneumophila.";
RL   Science 305:1966-1968(2004).
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; AE017354; AAU26828.1; -; Genomic_DNA.
DR   RefSeq; WP_010946476.1; NC_002942.5.
DR   RefSeq; YP_094775.1; NC_002942.5.
DR   ProteinModelPortal; Q5ZXJ2; -.
DR   SMR; Q5ZXJ2; -.
DR   STRING; 272624.lpg0739; -.
DR   PaxDb; Q5ZXJ2; -.
DR   EnsemblBacteria; AAU26828; AAU26828; lpg0739.
DR   GeneID; 19832304; -.
DR   KEGG; lpn:lpg0739; -.
DR   PATRIC; fig|272624.6.peg.762; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031446; -.
DR   KO; K01775; -.
DR   OMA; RDLELCS; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000609; 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    357       Alanine racemase.
FT                                /FTId=PRO_1000138610.
FT   ACT_SITE     35     35       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    256    256       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     131    131       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     304    304       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   357 AA;  39292 MW;  60C81F1EA5EDB2EF CRC64;
     MSRPTRLVIE PSALLHNLSQ IKHLAPGKKV IAMVKANAYG CGVREVAPVL DGRIEAFGVA
     CLEEALAIRA LGVETPCILF QGVFSSDELS VAVENDFACV LHHAQQLEWL IKTPLPYPIK
     VWVKVNTGMH RLGFKIHELQ KVMGALQTCT WVDKSIGLMT HLACADEPHR PENQQQISLF
     QEISIPGFRQ RSIANSAAII SFPDSQADVV RPGIMLYGVS PFANQNAHDL GLIPVMRFMS
     AISAIHDNPS FAQVGYGGTW KSDKPSRIGV VAAGYGDGYP RHISEKTPVW VRGREVSIVG
     RVSMDMLTID LTEHPDIEIG DEVELWGTHV LVERIAKSAG TVGYELLCQI SERVRYK
//
DBGET integrated database retrieval system