MURI_HELPJ
ID MURI_HELPJ Reviewed; 255 AA.
AC Q9ZLT0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 130.
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:19097892, ECO:0000269|PubMed:22877632};
GN Name=murI {ECO:0000255|HAMAP-Rule:MF_00258}; Synonyms=glr;
GN OrderedLocusNames=jhp_0496;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, CATALYTIC
RP ACTIVITY, SUBUNIT, FUNCTION, AND PATHWAY.
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 (1.87 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, CATALYTIC
RP ACTIVITY, AND SUBUNIT.
RX PubMed=19097892; DOI=10.1016/j.bmcl.2008.11.113;
RA Geng B., Basarab G., Comita-Prevoir J., Gowravaram M., Hill P., Kiely A.,
RA Loch J., MacPherson L., Morningstar M., Mullen G., Osimboni E., Satz A.,
RA Eyermann C., Lundqvist T.;
RT "Potent and selective inhibitors of Helicobacter pylori glutamate racemase
RT (MurI): pyridodiazepine amines.";
RL Bioorg. Med. Chem. Lett. 19:930-936(2009).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, AND
RP CATALYTIC ACTIVITY.
RX PubMed=22877632; DOI=10.1016/j.bmcl.2012.07.004;
RA Basarab G.S., Hill P., Eyermann C.J., Gowravaram M., Kack H., Osimoni E.;
RT "Design of inhibitors of Helicobacter pylori glutamate racemase as
RT selective antibacterial agents: incorporation of imidazoles onto a core
RT pyrazolopyrimidinedione scaffold to improve bioavailability.";
RL Bioorg. Med. Chem. Lett. 22:5600-5607(2012).
CC -!- FUNCTION: Provides the (R)-glutamate required for cell wall
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00258,
CC ECO:0000305|PubMed:17568739}.
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:19097892,
CC ECO:0000269|PubMed:22877632};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00258, ECO:0000269|PubMed:17568739}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17568739,
CC ECO:0000269|PubMed:19097892}.
CC -!- INTERACTION:
CC Q9ZLT0; Q9ZLT0: murI; NbExp=4; IntAct=EBI-15642574, EBI-15642574;
CC -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family.
CC {ECO:0000255|HAMAP-Rule:MF_00258}.
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DR EMBL; AE001439; AAD06074.1; -; Genomic_DNA.
DR PIR; C71924; C71924.
DR RefSeq; WP_000690367.1; NZ_CP011330.1.
DR PDB; 2JFX; X-ray; 2.30 A; A/B=1-255.
DR PDB; 2JFY; X-ray; 1.90 A; A/B=1-255.
DR PDB; 2JFZ; X-ray; 1.86 A; A/B=1-255.
DR PDB; 2W4I; X-ray; 1.87 A; A/B/E/F=1-255.
DR PDB; 4B1F; X-ray; 2.05 A; A/B=1-255.
DR PDBsum; 2JFX; -.
DR PDBsum; 2JFY; -.
DR PDBsum; 2JFZ; -.
DR PDBsum; 2W4I; -.
DR PDBsum; 4B1F; -.
DR AlphaFoldDB; Q9ZLT0; -.
DR SMR; Q9ZLT0; -.
DR DIP; DIP-60299N; -.
DR STRING; 85963.jhp_0496; -.
DR BindingDB; Q9ZLT0; -.
DR ChEMBL; CHEMBL5185; -.
DR DrugBank; DB08698; 1-[(3S)-5-PHENYL-3-THIOPHEN-2-YL-3H-1,4-BENZODIAZEPIN-2-YL]AZETIDIN-3-OL.
DR EnsemblBacteria; AAD06074; AAD06074; jhp_0496.
DR KEGG; hpj:jhp_0496; -.
DR PATRIC; fig|85963.30.peg.500; -.
DR eggNOG; COG0796; Bacteria.
DR OMA; LDFFKPH; -.
DR BRENDA; 5.1.1.3; 2604.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; Q9ZLT0; -.
DR Proteomes; UP000000804; 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.
FT CHAIN 1..255
FT /note="Glutamate racemase"
FT /id="PRO_0000095477"
FT ACT_SITE 70
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O58403, ECO:0000255|HAMAP-
FT Rule:MF_00258"
FT ACT_SITE 181
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O58403, ECO:0000255|HAMAP-
FT Rule:MF_00258"
FT BINDING 7..8
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258,
FT ECO:0000269|PubMed:17568739, ECO:0000269|PubMed:19097892,
FT ECO:0000269|PubMed:22877632, ECO:0007744|PDB:2JFX,
FT ECO:0007744|PDB:2JFY, ECO:0007744|PDB:2JFZ,
FT ECO:0007744|PDB:2W4I, ECO:0007744|PDB:4B1F"
FT BINDING 39..40
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258,
FT ECO:0000269|PubMed:17568739, ECO:0000269|PubMed:19097892,
FT ECO:0000269|PubMed:22877632, ECO:0007744|PDB:2JFX,
FT ECO:0007744|PDB:2JFY, ECO:0007744|PDB:2JFZ,
FT ECO:0007744|PDB:2W4I, ECO:0007744|PDB:4B1F"
FT BINDING 71..72
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258,
FT ECO:0000269|PubMed:17568739, ECO:0000269|PubMed:19097892,
FT ECO:0000269|PubMed:22877632, ECO:0007744|PDB:2JFX,
FT ECO:0007744|PDB:2JFY, ECO:0007744|PDB:2JFZ,
FT ECO:0007744|PDB:2W4I, ECO:0007744|PDB:4B1F"
FT BINDING 182..183
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258,
FT ECO:0000269|PubMed:17568739, ECO:0000269|PubMed:19097892,
FT ECO:0000269|PubMed:22877632, ECO:0007744|PDB:2JFX,
FT ECO:0007744|PDB:2JFY, ECO:0007744|PDB:2JFZ,
FT ECO:0007744|PDB:2W4I, ECO:0007744|PDB:4B1F"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:2JFZ"
FT HELIX 13..21
FT /evidence="ECO:0007829|PDB:2JFZ"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:2JFZ"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:2JFZ"
FT HELIX 44..58
FT /evidence="ECO:0007829|PDB:2JFZ"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:2JFZ"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:2JFZ"
FT HELIX 71..76
FT /evidence="ECO:0007829|PDB:2JFZ"
FT HELIX 78..84
FT /evidence="ECO:0007829|PDB:2JFZ"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:2W4I"
FT HELIX 94..103
FT /evidence="ECO:0007829|PDB:2JFZ"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:2JFZ"
FT HELIX 117..122
FT /evidence="ECO:0007829|PDB:2JFZ"
FT HELIX 124..131
FT /evidence="ECO:0007829|PDB:2JFZ"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:2JFZ"
FT HELIX 145..150
FT /evidence="ECO:0007829|PDB:2JFZ"
FT HELIX 157..167
FT /evidence="ECO:0007829|PDB:2JFZ"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:2JFZ"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:2JFZ"
FT HELIX 188..198
FT /evidence="ECO:0007829|PDB:2JFZ"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:2JFZ"
FT HELIX 210..221
FT /evidence="ECO:0007829|PDB:2JFZ"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:2W4I"
FT STRAND 233..240
FT /evidence="ECO:0007829|PDB:2JFZ"
FT HELIX 242..253
FT /evidence="ECO:0007829|PDB:2JFZ"
SQ SEQUENCE 255 AA; 28503 MW; B31F72E86EBAAC7B CRC64;
MKIGVFDSGV GGFSVLKSLL KARLFDEIIY YGDSARVPYG TKDPTTIKQF GLEALDFFKP
HEIELLIVAC NTASALALEE MQKYSKIPIV GVIEPSILAI KRQVEDKNAP ILVLGTKATI
QSNAYDNALK QQGYLNISHL ATSLFVPLIE ESILEGELLE TCMHYYFTPL EILPEVIILG
CTHFPLIAQK IEGYFMGHFA LPTPPLLIHS GDAIVEYLQQ KYALKNNACT FPKVEFHASG
DVIWLERQAK EWLKL
