ID MURI_CLOPS Reviewed; 260 AA. AC Q0SPY8; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 16-JUN-2009, entry version 27. DE RecName: Full=Glutamate racemase; DE EC=5.1.1.3; GN Name=murI; OrderedLocusNames=CPR_2572; OS Clostridium perfringens (strain SM101 / Type A). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=289380; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16825665; DOI=10.1101/gr.5238106; RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., RA DeBoy R.T., Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., RA Haft D.H., Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., RA Sullivan S.A., Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., RA Benton J., Radune D., Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., RA Billington S.J., Songer J.G., McClane B.A., Titball R.W., Rood J.I., RA Melville S.B., Paulsen I.T.; RT "Skewed genomic variability in strains of the toxigenic bacterial RT pathogen, Clostridium perfringens."; RL Genome Res. 16:1031-1040(2006). 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 http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000312; ABG85863.1; -; Genomic_DNA. DR RefSeq; YP_699819.1; -. DR GeneID; 4205022; -. DR GenomeReviews; CP000312_GR; CPR_2572. DR KEGG; cpr:CPR_2572; -. DR TIGR; CPR_2572; -. DR HOGENOM; Q0SPY8; -. DR OMA; Q0SPY8; AIWATPA. DR GO; GO:0008881; F:glutamate racemase activity; IEA:HAMAP. DR GO; GO:0007047; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR HAMAP; MF_00258; -; 1. DR InterPro; IPR015942; Asp/Glu/hydantoin_racemase. DR InterPro; IPR001920; Asp/Glu_race. DR InterPro; IPR018187; Asp/Glu_racemase_CS. DR InterPro; IPR004391; Glu_race. DR Gene3D; G3DSA:3.40.50.1860; Asp/Glu_race; 1. DR Pfam; PF01177; Asp_Glu_race; 1. 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 1 260 Glutamate racemase. FT /FTId=PRO_1000047561. SQ SEQUENCE 260 AA; 29203 MW; 189F0065E785DA84 CRC64; MQDDLKNAPI GFFDSGLGGL SVLRKALEMM PNENYIYYGD SKHAPYGEKT PQEIRSLSFN AIEFLIKKGA KAIVIACNTA TSAAAHDLRE YYKDIPIIGI EPALKPAIKL HETGSVIVMA TKATLTQEKF KNLMDKYGEH REVIPLPCPG LVEFIEAGNL EGEEVKNFLR EKLNPYMDRE ISSIVLGCTH YPFVKDVIQD IVGEKVDIID GSSGTIRELK RRLEENNMQS ELKKKGDLDI FNSLEDNKIL ELSKKLIEIK //