ID MURI_BUCBP Reviewed; 263 AA. AC P59574; DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 11-APR-2003, sequence version 1. DT 02-SEP-2026, entry version 117. 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=bbp_502; OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Erwiniaceae; Buchnera. OX NCBI_TaxID=224915; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bp; RX PubMed=12522265; DOI=10.1073/pnas.0235981100; RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.; RT "Reductive genome evolution in Buchnera aphidicola."; RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003). 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; AE016826; AAO27207.1; -; Genomic_DNA. DR RefSeq; WP_011091608.1; NC_004545.1. DR AlphaFoldDB; P59574; -. DR SMR; P59574; -. DR STRING; 224915.bbp_502; -. DR KEGG; bab:bbp_502; -. DR eggNOG; COG0796; Bacteria. DR HOGENOM; CLU_052344_2_0_6; -. DR OrthoDB; 9801055at2; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000601; Chromosome. DR GO; GO:0008881; F:glutamate racemase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule. DR FunFam; 3.40.50.1860:FF:000001; Glutamate racemase; 1. DR Gene3D; 3.40.50.1860; -; 2. DR HAMAP; MF_00258; Glu_racemase; 1. DR InterPro; IPR001920; Asp/Glu_race. 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 SUPFAM; SSF53681; Aspartate/glutamate racemase; 2. DR PROSITE; PS00924; ASP_GLU_RACEMASE_2; 1. PE 3: Inferred from homology; KW Cell shape; Cell wall biogenesis/degradation; Isomerase; KW Peptidoglycan synthesis; Reference proteome. FT CHAIN 1..263 FT /note="Glutamate racemase" FT /id="PRO_0000095461" FT ACT_SITE 75 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258" FT ACT_SITE 187 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 76..77 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258" FT BINDING 188..189 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258" SQ SEQUENCE 263 AA; 30533 MW; 628450BAE47C9752 CRC64; MNLKNYIIIF DSSLGGLSIY KQIKKKFPYM NYIYVCDNKN FPYGEKDEIF ILKRSIKIIS TITKKITTIL VILACNTITV TSLTTLKNFF NFPIIGVIPN LNKARKITKN NIIGLLGTKI TIHHYYIQNH ISLFVPKYKI KLLANNTLVK IAEQKIKNQL ISTKNIKFIL EPLLKKHNMP DTLILGCTHF SFLKEEIKKI FPKKIQIIDS KVHIPKNIST ILARNLKTTN NNIAFFSKKI ITTKTIHYLL KKYNFKKIKE LNT //