MURI_ENTFA
ID MURI_ENTFA Reviewed; 273 AA.
AC Q836J0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
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:17568739, ECO:0000269|PubMed:18614367};
GN Name=murI {ECO:0000255|HAMAP-Rule:MF_00258}; OrderedLocusNames=EF_1121;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH GLUTAMATE, CATALYTIC
RP ACTIVITY, AND SUBUNIT.
RX PubMed=17568739; DOI=10.1038/nature05689;
RA Lundqvist T., Fisher S.L., Kern G., Folmer R.H., Xue Y., Newton D.T.,
RA Keating T.A., Alm R.A., de Jonge B.L.;
RT "Exploitation of structural and regulatory diversity in glutamate
RT racemases.";
RL Nature 447:817-822(2007).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1-270 IN COMPLEX WITH
RP D-GLUTAMATE, AND CATALYTIC ACTIVITY.
RX PubMed=18614367; DOI=10.1016/j.bmcl.2008.06.068;
RA Geng B., Breault G., Comita-Prevoir J., Petrichko R., Eyermann C.,
RA Lundqvist T., Doig P., Gorseth E., Noonan B.;
RT "Exploring 9-benzyl purines as inhibitors of glutamate racemase (MurI) in
RT Gram-positive bacteria.";
RL Bioorg. Med. Chem. Lett. 18:4368-4372(2008).
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:17568739, ECO:0000269|PubMed:18614367};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00258}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17568739}.
CC -!- INTERACTION:
CC Q836J0; Q836J0: murI; NbExp=4; IntAct=EBI-15642753, EBI-15642753;
CC -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family.
CC {ECO:0000255|HAMAP-Rule:MF_00258}.
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DR EMBL; AE016830; AAO80921.1; -; Genomic_DNA.
DR RefSeq; NP_814851.1; NC_004668.1.
DR RefSeq; WP_010706575.1; NC_004668.1.
DR PDB; 2JFO; X-ray; 2.50 A; A/B=1-273.
DR PDB; 2JFP; X-ray; 1.98 A; A/B=1-273.
DR PDB; 2VVT; X-ray; 1.65 A; A/B=1-270.
DR PDBsum; 2JFO; -.
DR PDBsum; 2JFP; -.
DR PDBsum; 2VVT; -.
DR AlphaFoldDB; Q836J0; -.
DR SMR; Q836J0; -.
DR DIP; DIP-60301N; -.
DR STRING; 226185.EF_1121; -.
DR BindingDB; Q836J0; -.
DR ChEMBL; CHEMBL5298; -.
DR DrugBank; DB07937; 2-butoxy-9-(2,6-difluorobenzyl)-N-(2-morpholin-4-ylethyl)-9H-purin-6-amine.
DR EnsemblBacteria; AAO80921; AAO80921; EF_1121.
DR KEGG; efa:EF1121; -.
DR PATRIC; fig|226185.45.peg.2374; -.
DR eggNOG; COG0796; Bacteria.
DR HOGENOM; CLU_052344_0_2_9; -.
DR OMA; MPWGPRT; -.
DR BRENDA; 5.1.1.3; 2095.
DR SABIO-RK; Q836J0; -.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; Q836J0; -.
DR PRO; PR:Q836J0; -.
DR Proteomes; UP000001415; Chromosome.
DR GO; GO:0008881; F:glutamate racemase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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..273
FT /note="Glutamate racemase"
FT /id="PRO_1000047564"
FT ACT_SITE 74
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O58403, ECO:0000255|HAMAP-
FT Rule:MF_00258"
FT ACT_SITE 185
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O58403, ECO:0000255|HAMAP-
FT Rule:MF_00258"
FT BINDING 11..12
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258,
FT ECO:0000269|PubMed:17568739, ECO:0000269|PubMed:18614367,
FT ECO:0007744|PDB:2JFO, ECO:0007744|PDB:2JFP,
FT ECO:0007744|PDB:2VVT"
FT BINDING 43..44
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258,
FT ECO:0000269|PubMed:17568739, ECO:0000269|PubMed:18614367,
FT ECO:0007744|PDB:2JFO, ECO:0007744|PDB:2JFP,
FT ECO:0007744|PDB:2VVT"
FT BINDING 75..76
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258,
FT ECO:0000269|PubMed:17568739, ECO:0000269|PubMed:18614367,
FT ECO:0007744|PDB:2JFO, ECO:0007744|PDB:2JFP,
FT ECO:0007744|PDB:2VVT"
FT BINDING 186..187
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258,
FT ECO:0000269|PubMed:17568739, ECO:0000269|PubMed:18614367,
FT ECO:0007744|PDB:2JFO, ECO:0007744|PDB:2JFP,
FT ECO:0007744|PDB:2VVT"
FT HELIX 2..4
FT /evidence="ECO:0007829|PDB:2VVT"
FT STRAND 7..14
FT /evidence="ECO:0007829|PDB:2VVT"
FT HELIX 17..26
FT /evidence="ECO:0007829|PDB:2VVT"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:2VVT"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:2VVT"
FT HELIX 48..63
FT /evidence="ECO:0007829|PDB:2VVT"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:2VVT"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:2VVT"
FT HELIX 75..88
FT /evidence="ECO:0007829|PDB:2VVT"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:2VVT"
FT HELIX 98..107
FT /evidence="ECO:0007829|PDB:2VVT"
FT STRAND 109..117
FT /evidence="ECO:0007829|PDB:2VVT"
FT HELIX 119..123
FT /evidence="ECO:0007829|PDB:2VVT"
FT HELIX 126..132
FT /evidence="ECO:0007829|PDB:2VVT"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:2VVT"
FT HELIX 148..153
FT /evidence="ECO:0007829|PDB:2VVT"
FT HELIX 160..170
FT /evidence="ECO:0007829|PDB:2VVT"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:2VVT"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:2JFP"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:2VVT"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:2VVT"
FT HELIX 192..199
FT /evidence="ECO:0007829|PDB:2VVT"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:2VVT"
FT HELIX 208..222
FT /evidence="ECO:0007829|PDB:2VVT"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:2VVT"
FT HELIX 244..255
FT /evidence="ECO:0007829|PDB:2VVT"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:2VVT"
SQ SEQUENCE 273 AA; 29479 MW; 1F2ADF4D0B93991D CRC64;
MSNQEAIGLI DSGVGGLTVL KEALKQLPNE RLIYLGDTAR CPYGPRPAEQ VVQFTWEMAD
FLLKKRIKML VIACNTATAV ALEEIKAALP IPVVGVILPG ARAAVKVTKN NKIGVIGTLG
TIKSASYEIA IKSKAPTIEV TSLDCPKFVP IVESNQYRSS VAKKIVAETL QALQLKGLDT
LILGCTHYPL LRPVIQNVMG SHVTLIDSGA ETVGEVSMLL DYFDIAHTPE APTQPHEFYT
TGSAKMFEEI ASSWLGIENL KAQQIHLGGN END
