MURI_LIMFE
ID MURI_LIMFE Reviewed; 268 AA.
AC Q03469;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Glutamate racemase {ECO:0000255|HAMAP-Rule:MF_00258};
DE EC=5.1.1.3 {ECO:0000255|HAMAP-Rule:MF_00258, ECO:0000269|PubMed:10194325, ECO:0000269|PubMed:8097110, ECO:0000269|PubMed:8385993};
GN Name=murI {ECO:0000255|HAMAP-Rule:MF_00258};
OS Limosilactobacillus fermentum (Lactobacillus fermentum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=1613;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, CATALYTIC
RP ACTIVITY, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 9338 / DSM 20391 / JCM 1560 / NBRC 3071 / NCDO 215 / NCIMB 8028
RC / NCTC 6991 / 36;
RX PubMed=8385993; DOI=10.1021/bi00066a019;
RA Gallo K.A., Knowles J.R.;
RT "Purification, cloning, and cofactor independence of glutamate racemase
RT from Lactobacillus.";
RL Biochemistry 32:3981-3990(1993).
RN [2]
RP CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF CYS-73 AND CYS-184.
RX PubMed=8097110; DOI=10.1021/bi00066a021;
RA Tanner M.E., Gallo K.A., Knowles J.R.;
RT "Isotope effects and the identification of catalytic residues in the
RT reaction catalyzed by glutamate racemase.";
RL Biochemistry 32:3998-4006(1993).
RN [3]
RP CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF CYS-73 AND CYS-184.
RX PubMed=10194325; DOI=10.1021/bi982663n;
RA Glavas S., Tanner M.E.;
RT "Catalytic acid/base residues of glutamate racemase.";
RL Biochemistry 38:4106-4113(1999).
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 ECO:0000269|PubMed:10194325, ECO:0000269|PubMed:8097110,
CC ECO:0000269|PubMed:8385993};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.25 mM for (R)-glutamate {ECO:0000269|PubMed:8385993};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00258}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8385993}.
CC -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family.
CC {ECO:0000255|HAMAP-Rule:MF_00258}.
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DR EMBL; L02916; AAA25241.1; -; Genomic_DNA.
DR PIR; A49473; A49473.
DR RefSeq; WP_012390977.1; NZ_SMZH01000019.1.
DR AlphaFoldDB; Q03469; -.
DR SMR; Q03469; -.
DR STRING; 1613.GCA_002119645_00593; -.
DR BindingDB; Q03469; -.
DR ChEMBL; CHEMBL3353; -.
DR DrugCentral; Q03469; -.
DR GeneID; 61200454; -.
DR PATRIC; fig|1613.34.peg.2476; -.
DR BRENDA; 5.1.1.3; 2856.
DR SABIO-RK; Q03469; -.
DR UniPathway; UPA00219; -.
DR PRO; PR:Q03469; -.
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 Cell shape; Cell wall biogenesis/degradation; Direct protein sequencing;
KW Isomerase; Peptidoglycan synthesis.
FT CHAIN 1..268
FT /note="Glutamate racemase"
FT /id="PRO_0000095479"
FT ACT_SITE 73
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258,
FT ECO:0000269|PubMed:10194325, ECO:0000269|PubMed:8097110"
FT ACT_SITE 184
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258,
FT ECO:0000269|PubMed:10194325, ECO:0000269|PubMed:8097110"
FT BINDING 10..11
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22634, ECO:0000255|HAMAP-
FT Rule:MF_00258"
FT BINDING 42..43
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22634, ECO:0000255|HAMAP-
FT Rule:MF_00258"
FT BINDING 74..75
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22634, ECO:0000255|HAMAP-
FT Rule:MF_00258"
FT BINDING 185..186
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22634, ECO:0000255|HAMAP-
FT Rule:MF_00258"
FT MUTAGEN 73
FT /note="C->A: Abolishes racemase activity."
FT /evidence="ECO:0000269|PubMed:8097110"
FT MUTAGEN 73
FT /note="C->S: Reduces racemase activity 1000-fold."
FT /evidence="ECO:0000269|PubMed:10194325"
FT MUTAGEN 184
FT /note="C->A: Abolishes racemase activity."
FT /evidence="ECO:0000269|PubMed:8097110"
FT MUTAGEN 184
FT /note="C->S: Reduces racemase activity 1000-fold."
FT /evidence="ECO:0000269|PubMed:10194325"
SQ SEQUENCE 268 AA; 28314 MW; 6214F5817FFCEA61 CRC64;
MDNRPIGVMD SGLGGLSVVR VIQQKLPNEE VIFVGDQGHF PYGTKDQAEV RQLALSIGAF
LLKHDVKMMV VACNTATAAA LPALQAALPI PVIGVIEPGA RAALAQDKKG PIGVIATTAT
TTAGAYPATI ERLAPGTPVI AKATQPMVEI VEHGQTGTAK AQEVVSEQLM TFKEHPVKTL
IMGCTHFPFL APEISKAVGP TVALVDPAKE TVATAKSWLE QHQAMGNHAH PNYHLYSTGN
LPDLRAGVNK WLLSGHFDLG TAQIEEGD
