ID   MURI_BIFLS              Reviewed;         264 AA.
AC   B7GPZ1; E8MQV0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
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};
GN   OrderedLocusNames=Blon_0768, BLIJ_0783;
OS   Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM
OS   1222 / NCTC 11817 / S12).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=391904;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX   PubMed=19033196; DOI=10.1073/pnas.0809584105;
RA   Sela D.A., Chapman J., Adeuya A., Kim J.H., Chen F., Whitehead T.R.,
RA   Lapidus A., Rokhsar D.S., Lebrilla C.B., German J.B., Price N.P.,
RA   Richardson P.M., Mills D.A.;
RT   "The genome sequence of Bifidobacterium longum subsp. infantis reveals
RT   adaptations for milk utilization within the infant microbiome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:18964-18969(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX   PubMed=21270894; DOI=10.1038/nature09646;
RA   Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., Tobe T.,
RA   Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., Kikuchi J.,
RA   Morita H., Hattori M., Ohno H.;
RT   "Bifidobacteria can protect from enteropathogenic infection through
RT   production of acetate.";
RL   Nature 469:543-547(2011).
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; CP001095; ACJ51871.1; -; Genomic_DNA.
DR   EMBL; AP010889; BAJ68375.1; -; Genomic_DNA.
DR   RefSeq; WP_012577153.1; NZ_JDTT01000007.1.
DR   AlphaFoldDB; B7GPZ1; -.
DR   SMR; B7GPZ1; -.
DR   PRIDE; B7GPZ1; -.
DR   EnsemblBacteria; ACJ51871; ACJ51871; Blon_0768.
DR   KEGG; bln:Blon_0768; -.
DR   KEGG; blon:BLIJ_0783; -.
DR   PATRIC; fig|391904.8.peg.789; -.
DR   HOGENOM; CLU_052344_1_0_11; -.
DR   OMA; MPWGPRT; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001360; Chromosome.
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; IPR018187; Asp/Glu_racemase_AS_1.
DR   InterPro; IPR004391; Glu_race.
DR   Pfam; PF01177; Asp_Glu_race; 1.
DR   SUPFAM; SSF53681; SSF53681; 2.
DR   TIGRFAMs; TIGR00067; glut_race; 1.
DR   PROSITE; PS00923; ASP_GLU_RACEMASE_1; 1.
PE   3: Inferred from homology;
KW   Cell shape; Cell wall biogenesis/degradation; Isomerase;
KW   Peptidoglycan synthesis.
FT   CHAIN           1..264
FT                   /note="Glutamate racemase"
FT                   /id="PRO_1000125602"
FT   ACT_SITE        74
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   ACT_SITE        193
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         194..195
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
SQ   SEQUENCE   264 AA;  28972 MW;  21D3D74AFBF3E146 CRC64;
     MSSSAPIGVF DSGLGGISVA RQIAKDMPAE HVLYFGDSAN APYGIKTPEQ VRALSFDIVE
     RFVRQGVKAV VIACNTATSA AVNDLREHYD IPIIGMEPAL KVACDRGDVP SDPHHIPQRV
     IVAATPLTLR ERKFATLMDR FDSQNTIFKE PCPDLVEIVE SGRLGDHDLV MRTLHGYFDQ
     YDMEHIDSVV LGCTHFVFYR DYFRELLPER AAVIDGNEGT VRHLGVVLES LGKLAPEGAT
     GGVELANSDP SERIAELSRK LLNV