ID MURI_BACC2 Reviewed; 269 AA. AC B7IIZ3; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 1. DT 02-SEP-2026, entry version 90. 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=BCG9842_B0632; OS Bacillus cereus (strain G9842). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus; Bacillus cereus group. OX NCBI_TaxID=405531; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G9842; RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A., RA Ravel J., Sutton G.; RT "Genome sequence of Bacillus cereus G9842."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001186; ACK93718.1; -; Genomic_DNA. DR RefSeq; WP_000774005.1; NC_011772.1. DR AlphaFoldDB; B7IIZ3; -. DR SMR; B7IIZ3; -. DR GeneID; 50195275; -. DR KEGG; bcg:BCG9842_B0632; -. DR HOGENOM; CLU_052344_0_2_9; -. DR UniPathway; UPA00219; -. DR GO; GO:0008881; F:glutamate racemase activity; IEA:UniProtKB-UniRule. DR GO; GO:0042802; F:identical protein binding; IEA:UniProtKB-ARBA. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule. DR FunFam; 3.40.50.1860:FF:000002; Glutamate racemase; 1. DR Gene3D; 3.40.50.1860; -; 2. 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 NCBIfam; TIGR00067; glut_race; 1. DR NCBIfam; NF002035; PRK00865.1-3; 1. DR PANTHER; PTHR21198; GLUTAMATE RACEMASE; 1. DR PANTHER; PTHR21198:SF2; GLUTAMATE RACEMASE; 1. DR Pfam; PF01177; Asp_Glu_race; 1. DR SUPFAM; SSF53681; Aspartate/glutamate racemase; 2. 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..269 FT /note="Glutamate racemase" FT /id="PRO_1000119181" FT ACT_SITE 74 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258" FT ACT_SITE 185 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 186..187 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258" SQ SEQUENCE 269 AA; 29882 MW; 67328BB111B94A20 CRC64; MKLNRAIGVI DSGVGGLTVA KELIRQLPKE RIIYLGDTAR CPYGPRSREE VRQFTWEMTE HLLDLNIKML VIACNTATAV VLEEMQKQLP IPVVGVIHPG SRTALKVTNT YHVGIIGTIG TVKSGAYEEA LKSINNRVMV ESLACPPFVE LVESGNFESE MAYEVVRETL QPLKSTDIDT LILGCTHYPI LGPVIKKVMG DKVQLISSGD ETAREVSTIL YHSKMLNEGE EQSDHLFLTT GKIGLFKEIA SKWFGQPIEN VKHIHLEKE //