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 10-AUG-2010, entry version 17. DE RecName: Full=Glutamate racemase; DE EC=5.1.1.3; GN Name=murI; OrderedLocusNames=PMI3247; OS Proteus mirabilis (strain HI4320). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Proteus. OX NCBI_TaxID=529507; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 (By similarity). CC -!- CATALYTIC ACTIVITY: L-glutamate = D-glutamate. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family. 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; YP_002152932.1; -. DR GeneID; 6802950; -. DR GenomeReviews; AM942759_GR; PMI3247. DR HOGENOM; HBG645102; -. DR OMA; CGHIPYG; -. DR ProtClustDB; PRK00865; -. DR GO; GO:0008881; F:glutamate racemase activity; IEA:EC. DR GO; GO:0007047; P:cellular cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW. 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. DR InterPro; IPR004391; Glu_race. DR Gene3D; G3DSA:3.40.50.1860; Asp/Glu_race; 1. DR Pfam; PF01177; Asp_Glu_race; 1. DR SUPFAM; SSF53681; Asp/Glu_race; 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. FT CHAIN 1 288 Glutamate racemase. FT /FTId=PRO_1000114058. 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 //