ID   MURI_LACE2              Reviewed;         265 AA.
AC   C4Z114;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=EUBELI_01280;
OS   Lachnospira eligens (strain ATCC 27750 / DSM 3376 / VPI C15-48 / C15-B4)
OS   (Eubacterium eligens).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Lachnospira.
OX   NCBI_TaxID=515620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27750 / DSM 3376 / VPI C15-48 / C15-B4;
RX   PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA   Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA   Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA   Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA   Hettich R.L., Gordon J.I.;
RT   "Characterizing a model human gut microbiota composed of members of its two
RT   dominant bacterial phyla.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
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; CP001104; ACR72277.1; -; Genomic_DNA.
DR   RefSeq; WP_012739512.1; NC_012778.1.
DR   AlphaFoldDB; C4Z114; -.
DR   SMR; C4Z114; -.
DR   STRING; 515620.EUBELI_01280; -.
DR   EnsemblBacteria; ACR72277; ACR72277; EUBELI_01280.
DR   GeneID; 41355997; -.
DR   KEGG; eel:EUBELI_01280; -.
DR   eggNOG; COG0796; Bacteria.
DR   HOGENOM; CLU_052344_1_0_9; -.
DR   OMA; KAVMIAC; -.
DR   OrthoDB; 1718671at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001476; 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; Reference proteome.
FT   CHAIN           1..265
FT                   /note="Glutamate racemase"
FT                   /id="PRO_1000204627"
FT   ACT_SITE        70
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         7..8
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         39..40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         71..72
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   265 AA;  29984 MW;  2B11C151185920FB CRC64;
     MKIGIFDSGI GGLSVLHQAM ITMPEADYIF YADVDNVPYG EKTREEVRKL VDHAVGFLVD
     KGCQAIVLAC NTATSAAISY LREKYKLPII GIEPAVKPAV EHTSETGRRV MVVSTPVTAK
     GEKLKRLIDK YDDKHVVDVV ALPKLVRFAQ DDDFDSSDVT DYLKCEFAPY NLNDYSELVL
     GCTHFNYFKD SFAKLFPDDL EMVDGNTGVS NNLKNTVMKK GIFTEKDKGK KGSVEYYYSD
     RKMESEAEMK HIKKLHERLE RMRQI