MURI_CLOB6
ID MURI_CLOB6 Reviewed; 257 AA.
AC C3KWB8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=CLJ_B3893;
OS Clostridium botulinum (strain 657 / Type Ba4).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=515621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=657 / Type Ba4;
RA Shrivastava S., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.S.;
RT "Genome sequence of Clostridium botulinum Ba4 strain 657.";
RL Submitted (MAY-2008) 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; CP001083; ACQ53971.1; -; Genomic_DNA.
DR RefSeq; WP_003361750.1; NC_012658.1.
DR AlphaFoldDB; C3KWB8; -.
DR SMR; C3KWB8; -.
DR EnsemblBacteria; ACQ53971; ACQ53971; CLJ_B3893.
DR KEGG; cbi:CLJ_B3893; -.
DR HOGENOM; CLU_052344_1_0_9; -.
DR OMA; LDFFKPH; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002333; 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 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 3: Inferred from homology;
KW Cell shape; Cell wall biogenesis/degradation; Isomerase;
KW Peptidoglycan synthesis.
FT CHAIN 1..257
FT /note="Glutamate racemase"
FT /id="PRO_1000204624"
FT ACT_SITE 75
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT ACT_SITE 185
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 186..187
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
SQ SEQUENCE 257 AA; 28813 MW; C2FF51D5496108F8 CRC64;
MSINDKPIGF FDSGVGGISV LKEAFKLLPK EDFLYYGDSK NTPYGTKKVE EVKALTFNAT
DFLMSKGIKA LVVACNTATS VTINDLRENY DIPIIGIEPA LKPAVELKKG GKIIIMATPM
TLAEKKFANL MDLYKETEDI EPLPCPGLPE LIEQGIVSGD VIYNYLKDKF SKYDDEKISS
IVLGCTHYPF VEETLKEVTH NKACIIDGSF GTSRELKRQL KNSNMLREEN RVGKVTIFNS
REDKDIIDLS YKLFNMK
