ID MURI_HERA2 Reviewed; 254 AA. AC A9AXC6; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 1. DT 02-SEP-2026, entry version 95. 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=Haur_4214; OS Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95). OC Bacteria; Bacillati; Chloroflexota; Chloroflexia; Herpetosiphonales; OC Herpetosiphonaceae; Herpetosiphon. OX NCBI_TaxID=316274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23779 / DSM 785 / 114-95; RX PubMed=22675585; DOI=10.4056/sigs.2194987; RA Kiss H., Nett M., Domin N., Martin K., Maresca J.A., Copeland A., RA Lapidus A., Lucas S., Berry K.W., Glavina Del Rio T., Dalin E., Tice H., RA Pitluck S., Richardson P., Bruce D., Goodwin L., Han C., Detter J.C., RA Schmutz J., Brettin T., Land M., Hauser L., Kyrpides N.C., Ivanova N., RA Goeker M., Woyke T., Klenk H.P., Bryant D.A.; RT "Complete genome sequence of the filamentous gliding predatory bacterium RT Herpetosiphon aurantiacus type strain (114-95(T))."; RL Stand. Genomic Sci. 5:356-370(2011). 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; CP000875; ABX06846.1; -; Genomic_DNA. DR AlphaFoldDB; A9AXC6; -. DR SMR; A9AXC6; -. DR FunCoup; A9AXC6; 236. DR STRING; 316274.Haur_4214; -. DR KEGG; hau:Haur_4214; -. DR eggNOG; COG0796; Bacteria. DR HOGENOM; CLU_052344_1_0_0; -. DR InParanoid; A9AXC6; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000787; 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; 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 NCBIfam; TIGR00067; glut_race; 1. DR PANTHER; PTHR21198; GLUTAMATE RACEMASE; 1. DR PANTHER; PTHR21198:SF2; GLUTAMATE RACEMASE; 1. DR Pfam; PF01177; Asp_Glu_race; 1. DR SUPFAM; SSF53681; Aspartate/glutamate racemase; 2. 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; Isomerase; KW Peptidoglycan synthesis; Reference proteome. FT CHAIN 1..254 FT /note="Glutamate racemase" FT /id="PRO_1000114049" FT ACT_SITE 73 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258" FT ACT_SITE 183 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258" FT BINDING 10..11 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258" FT BINDING 42..43 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258" FT BINDING 74..75 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258" FT BINDING 184..185 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258" SQ SEQUENCE 254 AA; 27269 MW; 978ADF7982E2239A CRC64; MKDQPIGMFD SGVGGLSTLR DLRALLPHED IIYYADTGNC PYGGRSHEEI VALSERITYI LLERGVKLIV VACNTATLHA VDYLREHFSI SFVGMEPGIK PAIAQTKTGV VGVMATQATV AGERFQRLIA RYAGDVQVVP QACPGLVELI EAGELQSETT RDAVARYVAP LLKAGADTIV LGCTHYPFLR SLIADVAGPN VALLDTGAAV ARQTQRLLAA ADLLNPQTSQ GSIEWLTSGD PAHFAKIRQC LEIE //