ID   MURI_LEPBJ              Reviewed;         258 AA.
AC   Q04QQ5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Glutamate racemase {ECO:0000255|HAMAP-Rule:MF_00258};
DE            EC=5.1.1.3 {ECO:0000255|HAMAP-Rule:MF_00258};
GN   Name=murI {ECO:0000255|HAMAP-Rule:MF_00258}; OrderedLocusNames=LBJ_2292;
OS   Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=355277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB197;
RX   PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA   Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA   Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA   Rood J.I., Davies J.K., Adler B.;
RT   "Genome reduction in Leptospira borgpetersenii reflects limited
RT   transmission potential.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
CC   -!- FUNCTION: Provides the (R)-glutamate required for cell wall
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00258}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamate = D-glutamate; Xref=Rhea:RHEA:12813,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:29986; EC=5.1.1.3;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00258};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00258}.
CC   -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family.
CC       {ECO:0000255|HAMAP-Rule:MF_00258}.
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DR   EMBL; CP000350; ABJ76765.1; -; Genomic_DNA.
DR   RefSeq; WP_011669676.1; NC_008510.1.
DR   AlphaFoldDB; Q04QQ5; -.
DR   SMR; Q04QQ5; -.
DR   EnsemblBacteria; ABJ76765; ABJ76765; LBJ_2292.
DR   KEGG; lbj:LBJ_2292; -.
DR   HOGENOM; CLU_052344_1_0_12; -.
DR   OMA; MPWGPRT; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000656; Chromosome 1.
DR   GO; GO:0008881; F:glutamate racemase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   HAMAP; MF_00258; Glu_racemase; 1.
DR   InterPro; IPR015942; Asp/Glu/hydantoin_racemase.
DR   InterPro; IPR001920; Asp/Glu_race.
DR   InterPro; IPR004391; Glu_race.
DR   Pfam; PF01177; Asp_Glu_race; 1.
DR   SUPFAM; SSF53681; SSF53681; 2.
DR   TIGRFAMs; TIGR00067; glut_race; 1.
PE   3: Inferred from homology;
KW   Cell shape; Cell wall biogenesis/degradation; Isomerase;
KW   Peptidoglycan synthesis.
FT   CHAIN           1..258
FT                   /note="Glutamate racemase"
FT                   /id="PRO_1000047580"
FT   ACT_SITE        74
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   ACT_SITE        182
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         11..12
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         43..44
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         75..76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         183..184
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
SQ   SEQUENCE   258 AA;  28796 MW;  F3754E453FE7AE54 CRC64;
     MKGPLKIGLM DSGMGGLSVL KGILKYDAEL EVVYYGDLKN SPYGEKETSE ILELVRDVCK
     RLQEENVSAI LLACNTATSA AAQTLRKEFS IPIFGMEPAI KPAILQNPGK KIALLATPVT
     QREKKLQRLK AELGAEELIL PVSCPGLAGL VDKGEFDEAE KYLRPILKKL REENVENLVL
     GCTHYIFLKH IILKNFPNVR IYDGNSGTIK HLLNSLQVRQ RVSNRSSVSG SVYKLILNSD
     EELHFRLATE LLQFENKF