ID MURI_BRUAB Reviewed; 277 AA. AC Q57CU6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2005, sequence version 1. DT 02-SEP-2026, entry version 105. 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=BruAb1_1200; OS Brucella abortus biovar 1 (strain 9-941). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group; Brucella; OC Brucella melitensis group. OX NCBI_TaxID=262698; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=9-941; RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005; RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.; RT "Completion of the genome sequence of Brucella abortus and comparison to RT the highly similar genomes of Brucella melitensis and Brucella suis."; RL J. Bacteriol. 187:2715-2726(2005). 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; AE017223; AAX74538.1; -; Genomic_DNA. DR RefSeq; WP_002964323.1; NC_006932.1. DR AlphaFoldDB; Q57CU6; -. DR SMR; Q57CU6; -. DR EnsemblBacteria; AAX74538; AAX74538; BruAb1_1200. DR GeneID; 93016476; -. DR GeneID; 99643607; -. DR KEGG; bmb:BruAb1_1200; -. DR HOGENOM; CLU_052344_2_0_5; -. DR UniPathway; UPA00219; -. DR GO; GO:0008881; F:glutamate racemase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule. 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 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..277 FT /note="Glutamate racemase" FT /id="PRO_1000047550" FT ACT_SITE 89 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258" FT ACT_SITE 204 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258" FT BINDING 25..26 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258" FT BINDING 57..58 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258" FT BINDING 90..91 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258" FT BINDING 205..206 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258" SQ SEQUENCE 277 AA; 30708 MW; B946C8EA5DD039E6 CRC64; MKKAPAGSFP AKPTIAPERP ILVFDSGIGG LTVLREARVV MPDRRFVYIA DDAGFPYGNW EEEALKRRII ELFGEFIANY DPEIAVIACN TASTLVLEDL RRAYPSVPFV GTVPAIKPAA ERTSSGLVSV LATPGTVKRA YTRDLIQSFA SRCHVRLVGA DGLAAIAEAH IRGESFDEAL VMAQIAPCFI EKDGKRTDIV VLACTHYPFL VNVLRRLAPW PVDWLDPAEA IARRMKSLLP ARSDDDEFHS QDDLAFFTSR KPDYAIRRLM QGFGLRF //