ID   MURI_PEDPE              Reviewed;         265 AA.
AC   Q08783;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 97.
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};
OS   Pediococcus pentosaceus.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Pediococcus.
OX   NCBI_TaxID=1255;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7904596; DOI=10.1128/jb.176.2.528-530.1994;
RA   Pucci M.J., Novotny J., Discotto L.F., Dougherty T.J.;
RT   "The Escherichia coli Dga (MurI) protein shares biological activity and
RT   structural domains with the Pediococcus pentosaceus glutamate racemase.";
RL   J. Bacteriol. 176:528-530(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7937852; DOI=10.1073/pnas.91.21.10144;
RA   Choi S., Esaki N., Ashiuchi M., Yoshimura T., Soda K.;
RT   "Bacterial glutamate racemase has high sequence similarity with myoglobins
RT   and forms an equimolar inactive complex with hemin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:10144-10147(1994).
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; L22789; AAA16761.1; -; Unassigned_DNA.
DR   EMBL; L22448; AAC36914.1; -; Genomic_DNA.
DR   RefSeq; WP_011673575.1; NZ_WEPA01000004.1.
DR   AlphaFoldDB; Q08783; -.
DR   SMR; Q08783; -.
DR   GeneID; 33061810; -.
DR   OMA; MPWGPRT; -.
DR   UniPathway; UPA00219; -.
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; IPR033134; Asp/Glu_racemase_AS_2.
DR   InterPro; IPR004391; Glu_race.
DR   PANTHER; PTHR21198:SF2; PTHR21198:SF2; 1.
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.
DR   PROSITE; PS00924; ASP_GLU_RACEMASE_2; 1.
PE   3: Inferred from homology;
KW   Cell shape; Cell wall biogenesis/degradation; Isomerase;
KW   Peptidoglycan synthesis.
FT   CHAIN           1..265
FT                   /note="Glutamate racemase"
FT                   /id="PRO_0000095496"
FT   ACT_SITE        73
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   ACT_SITE        184
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         10..11
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         42..43
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         74..75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         185..186
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
SQ   SEQUENCE   265 AA;  28976 MW;  9A2FC7841AECECC8 CRC64;
     MDNRPIGFMD SGVGGLTVVK TAQKLLPNEE IIFIGDEARM PYGPRPTAEV VEFSRQMASF
     LMTKNIKALV IACNTATNAA LAVLQAELPI PVIGVILPGA IAANRQTKNQ KIGVIATLGT
     IKSEAYPKAL AEINTKLRAY PVACQEFVEI AEKNELHTTA AQKVMNEKLA EFRQDQIDTL
     ILGCTHFPLL EEGIQAAVGP DVTLVDPGVE TVHQLIEILT KQALQHAEGP KAQDQYYSTG
     NIKNFEEIAR TFLNQDLRVE EVKID