ID MURI_PROMH Reviewed; 288 AA. AC B4F1H6; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 1. DT 15-MAR-2017, entry version 55. 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=PMI3247; OS Proteus mirabilis (strain HI4320). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Morganellaceae; Proteus. OX NCBI_TaxID=529507; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HI4320; RX PubMed=18375554; DOI=10.1128/JB.01981-07; RA Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S., RA Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T., RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H., RA Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N., RA Parkhill J., Mobley H.L.T.; RT "Complete genome sequence of uropathogenic Proteus mirabilis, a master RT of both adherence and motility."; RL J. Bacteriol. 190:4027-4037(2008). CC -!- FUNCTION: Provides the (R)-glutamate required for cell wall CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00258}. CC -!- CATALYTIC ACTIVITY: L-glutamate = D-glutamate. {ECO:0000255|HAMAP- CC 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; AM942759; CAR46364.1; -; Genomic_DNA. DR RefSeq; WP_012368686.1; NC_010554.1. DR ProteinModelPortal; B4F1H6; -. DR SMR; B4F1H6; -. DR STRING; 529507.PMI3247; -. DR EnsemblBacteria; CAR46364; CAR46364; PMI3247. DR GeneID; 6802950; -. DR KEGG; pmr:PMI3247; -. DR PATRIC; 20521172; VBIProMir120933_3174. DR eggNOG; ENOG4105F03; Bacteria. DR eggNOG; COG0796; LUCA. DR HOGENOM; HOG000262397; -. DR KO; K01776; -. DR OMA; WPVDWID; -. DR OrthoDB; POG091H00P1; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000008319; Chromosome. DR GO; GO:0008881; F:glutamate racemase activity; IEA:UniProtKB-EC. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1860; -; 1. 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:SF9; PTHR21198:SF9; 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; Complete proteome; KW Isomerase; Peptidoglycan synthesis; Reference proteome. FT CHAIN 1 288 Glutamate racemase. FT /FTId=PRO_1000114058. FT REGION 32 33 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00258}. FT REGION 64 65 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00258}. FT REGION 97 98 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00258}. FT REGION 210 211 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00258}. FT ACT_SITE 96 96 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00258}. FT ACT_SITE 209 209 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00258}. SQ SEQUENCE 288 AA; 31709 MW; 368F4E633C7EF3E6 CRC64; MAIARQDVNI SSPEATTSDA QSTANPTVLV FDSGVGGLSI YREIREKLPD AHYIYVFDNE AFPYGEKPQE FIIERVVRIV SAVAQQHELA AIVIACNTAS TVSLPALRAK FTDIPIVGVV PAIKPAAKLT CNGVVGLLAT RATVKRPYTH ELIERFATEC KVHLLGSAEL VELAEKKLHG EKVSCDELRR ILAPWLKMKE PPDTVVLGCT HFPLLEEELL SVLPDGTRII DSGGAIARRT AWLVVNQDKI RGSKEISFAY CLKEDEYSEL LKPVLADFGF KMLRKLAL //