ID MURI_THET8 Reviewed; 257 AA. AC Q5SHT7; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 02-SEP-2026, entry version 120. 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=TTHA1643; OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8). OC Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales; Thermaceae; OC Thermus. OX NCBI_TaxID=300852; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27634 / DSM 579 / HB8; RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.; RT "Complete genome sequence of Thermus thermophilus HB8."; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. 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; AP008226; BAD71466.1; -; Genomic_DNA. DR RefSeq; WP_011228827.1; NC_006461.1. DR PDB; 5W16; X-ray; 1.91 A; A/B/C/D=2-257. DR PDB; 6DLI; X-ray; 2.70 A; A/B/C/D=2-257. DR AlphaFoldDB; Q5SHT7; -. DR SMR; Q5SHT7; -. DR EnsemblBacteria; BAD71466; BAD71466; BAD71466. DR GeneID; 3169688; -. DR KEGG; ttj:TTHA1643; -. DR PATRIC; fig|300852.9.peg.1613; -. DR eggNOG; COG0796; Bacteria. DR HOGENOM; CLU_052344_0_2_0; -. DR PhylomeDB; Q5SHT7; -. DR BRENDA; 5.1.1.3; 2305. DR UniPathway; UPA00219; -. DR Proteomes; UP000000532; 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:000002; 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. DR PDBsum; 5W16; -. DR PDBsum; 6DLI; -. PE 1: Evidence at protein level; KW 3D-structure; Cell shape; Cell wall biogenesis/degradation; Isomerase; KW Peptidoglycan synthesis; Reference proteome. FT CHAIN 1..257 FT /note="Glutamate racemase" FT /id="PRO_1000078584" FT ACT_SITE 75 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258" FT ACT_SITE 176 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258" FT BINDING 12..13 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258" FT BINDING 44..45 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258" FT BINDING 76..77 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258" FT BINDING 177..178 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258" FT STRAND 8..15 FT /evidence="ECO:0007829|PDB:5W16" FT HELIX 18..27 FT /evidence="ECO:0007829|PDB:5W16" FT STRAND 33..37 FT /evidence="ECO:0007829|PDB:5W16" FT TURN 39..41 FT /evidence="ECO:0007829|PDB:6DLI" FT HELIX 49..65 FT /evidence="ECO:0007829|PDB:5W16" FT STRAND 69..73 FT /evidence="ECO:0007829|PDB:5W16" FT HELIX 76..82 FT /evidence="ECO:0007829|PDB:5W16" FT HELIX 85..89 FT /evidence="ECO:0007829|PDB:5W16" FT STRAND 90..92 FT /evidence="ECO:0007829|PDB:5W16" FT HELIX 99..105 FT /evidence="ECO:0007829|PDB:5W16" FT STRAND 108..115 FT /evidence="ECO:0007829|PDB:5W16" FT HELIX 117..122 FT /evidence="ECO:0007829|PDB:5W16" FT HELIX 125..127 FT /evidence="ECO:0007829|PDB:5W16" FT STRAND 132..136 FT /evidence="ECO:0007829|PDB:5W16" FT HELIX 140..145 FT /evidence="ECO:0007829|PDB:5W16" FT STRAND 149..151 FT /evidence="ECO:0007829|PDB:6DLI" FT HELIX 152..162 FT /evidence="ECO:0007829|PDB:5W16" FT STRAND 171..176 FT /evidence="ECO:0007829|PDB:5W16" FT HELIX 179..182 FT /evidence="ECO:0007829|PDB:5W16" FT HELIX 183..189 FT /evidence="ECO:0007829|PDB:5W16" FT STRAND 194..197 FT /evidence="ECO:0007829|PDB:5W16" FT HELIX 198..212 FT /evidence="ECO:0007829|PDB:5W16" FT STRAND 224..230 FT /evidence="ECO:0007829|PDB:5W16" FT HELIX 232..241 FT /evidence="ECO:0007829|PDB:5W16" FT STRAND 248..251 FT /evidence="ECO:0007829|PDB:5W16" FT HELIX 254..256 FT /evidence="ECO:0007829|PDB:5W16" SQ SEQUENCE 257 AA; 27656 MW; 048F2B8DE59669B1 CRC64; MKDPKAPIGV FDSGVGGLTV LKALRRLLPR EEFLYFGDTA RVPYGGKPLA MVRRFAWEIA GFLLRQGVKA IVVACNTASS AALPDLAEDL SVPVFGVVEP AARAARGFRK VGLIGTQATV ESGAYPRYVD LAWAKACPLF VPLVEEGLWD DPVALLVARH YLEDAPKDLE ALILGCTHYP FLKGAIGAVL PGVALLDSAE LTAQEVARAL EAEGLLNPEG RGRTFHLVTG DPEAYRALAE RLGERVEAVR RVSLEEL //