MURI_THET8
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 03-AUG-2022, entry version 109.
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}; OrderedLocusNames=TTHA1643;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; 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}.
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DR EMBL; AP008226; BAD71466.1; -; Genomic_DNA.
DR RefSeq; WP_011228827.1; NC_006461.1.
DR RefSeq; YP_144909.1; 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 PDBsum; 5W16; -.
DR PDBsum; 6DLI; -.
DR AlphaFoldDB; Q5SHT7; -.
DR SMR; Q5SHT7; -.
DR STRING; 300852.55773025; -.
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 OMA; MPWGPRT; -.
DR PhylomeDB; Q5SHT7; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0008881; F:glutamate racemase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
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_1.
DR InterPro; IPR033134; Asp/Glu_racemase_AS_2.
DR InterPro; IPR004391; Glu_race.
DR PANTHER; PTHR21198:SF2; PTHR21198:SF2; 1.
DR Pfam; PF01177; Asp_Glu_race; 1.
DR SUPFAM; SSF53681; SSF53681; 2.
DR TIGRFAMs; TIGR00067; glut_race; 1.
DR PROSITE; PS00923; ASP_GLU_RACEMASE_1; 1.
DR PROSITE; PS00924; ASP_GLU_RACEMASE_2; 1.
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:6DLI"
FT HELIX 18..27
FT /evidence="ECO:0007829|PDB:6DLI"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:6DLI"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:6DLI"
FT HELIX 49..66
FT /evidence="ECO:0007829|PDB:6DLI"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:6DLI"
FT HELIX 76..82
FT /evidence="ECO:0007829|PDB:6DLI"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:6DLI"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:6DLI"
FT HELIX 99..105
FT /evidence="ECO:0007829|PDB:6DLI"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:6DLI"
FT HELIX 117..122
FT /evidence="ECO:0007829|PDB:6DLI"
FT TURN 123..128
FT /evidence="ECO:0007829|PDB:6DLI"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:6DLI"
FT HELIX 140..145
FT /evidence="ECO:0007829|PDB:6DLI"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:6DLI"
FT HELIX 152..161
FT /evidence="ECO:0007829|PDB:6DLI"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:6DLI"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:6DLI"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:6DLI"
FT HELIX 183..189
FT /evidence="ECO:0007829|PDB:6DLI"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:6DLI"
FT HELIX 198..213
FT /evidence="ECO:0007829|PDB:6DLI"
FT STRAND 224..230
FT /evidence="ECO:0007829|PDB:6DLI"
FT HELIX 232..241
FT /evidence="ECO:0007829|PDB:6DLI"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:6DLI"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:6DLI"
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
