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Database: UniProt
Entry: Q8XZM4
LinkDB: Q8XZM4
Original site: Q8XZM4 
ID   ALR_RALSO               Reviewed;         375 AA.
AC   Q8XZM4;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 1.
DT   16-JAN-2019, entry version 107.
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=RSc1371; ORFNames=RS04748;
OS   Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=267608;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GMI1000;
RX   PubMed=11823852; DOI=10.1038/415497a;
RA   Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S.,
RA   Arlat M., Billault A., Brottier P., Camus J.-C., Cattolico L.,
RA   Chandler M., Choisne N., Claudel-Renard C., Cunnac S., Demange N.,
RA   Gaspin C., Lavie M., Moisan A., Robert C., Saurin W., Schiex T.,
RA   Siguier P., Thebault P., Whalen M., Wincker P., Levy M.,
RA   Weissenbach J., Boucher C.A.;
RT   "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL   Nature 415:497-502(2002).
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; AL646052; CAD15073.1; -; Genomic_DNA.
DR   RefSeq; WP_011001320.1; NC_003295.1.
DR   ProteinModelPortal; Q8XZM4; -.
DR   SMR; Q8XZM4; -.
DR   STRING; 267608.RSc1371; -.
DR   EnsemblBacteria; CAD15073; CAD15073; RSc1371.
DR   GeneID; 1220195; -.
DR   KEGG; rso:RSc1371; -.
DR   PATRIC; fig|267608.8.peg.1397; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031446; -.
DR   KO; K01775; -.
DR   OMA; RDLELCS; -.
DR   BioCyc; RSOL267608:RS_RS06875-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000001436; 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; 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; Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    375       Alanine racemase.
FT                                /FTId=PRO_0000114550.
FT   ACT_SITE     35     35       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    253    253       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     130    130       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      35     35       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   375 AA;  40103 MW;  636F7E7F5026DDD6 CRC64;
     MPRPIQAVIH GPALVNNLQV VRRHAADSRV WAVIKANAYG HGIERAYEGL RQADGFGLLD
     LDEAVRLRQL GWQGPILLLE GFFKPEDLAL VEQYRLTTTV HCEEQLRMLE LARLKGPVSI
     QLKINTGMSR LGFAPAAYRA AWEHARAISG IGTIVHMTHF SDADGPRGID HQLAAFEQAT
     QGLPGEASLS NSAATLWHPR AHRDWVRPGV ILYGASPTGV AADIEGTGLM PAMTLKSELI
     AVQDLQPGAT VGYGSRFEAE QPMRIGIVAC GYADGYPRHA PGWDGNYTPV LVDGVRTRMV
     GRVSMDMITV DLAEVPGARV GAPVTLWGQG LPIDEVAHAA GTVGYELMCA LAPRVPVTVE
     PAGAADAGET LGKAA
//
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