ID MURI_CLOP1 Reviewed; 260 AA. AC Q0TM83; 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=CPF_2893; OS Clostridium perfringens (strain ATCC 13124 / NCTC 8237 / Type A). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=195103; 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; CP000246; ABG84145.1; -; Genomic_DNA. DR RefSeq; YP_697257.1; -. DR GeneID; 4203366; -. DR GenomeReviews; CP000246_GR; CPF_2893. DR KEGG; cpf:CPF_2893; -. DR TIGR; CPF_2893; -. DR HOGENOM; Q0TM83; -. DR OMA; Q0TM83; 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_1000047560. SQ SEQUENCE 260 AA; 29177 MW; 300EFBEE64156543 CRC64; MQDDLKNAPI GFFDSGLGGL SVLRKALEMM PNENYIYYGD SKHAPYGEKT PQEIRSLSFN AIEFLIKKGA KAIVIACNTA TSAAAHDLRE YYKDIPIIGI EPALKPAIKL HETGSVIVMA TKATLNQEKF KNLMDKYGEH REVIPLPCPG LVEFIEAGDL EGEDVKNFLR EKLNPYMDRE ISSIVLGCTH YPFVKDVIQD IVGEKVDIID GSSGTVRELK RRLEENNMES ESKKKGNLDI FNSLEDKKIL ELSKKLIEIK //