MURI_STRP1
ID MURI_STRP1 Reviewed; 264 AA.
AC Q9A1B7; Q490P6;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
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:17658548};
GN Name=murI {ECO:0000255|HAMAP-Rule:MF_00258}; Synonyms=glr;
GN OrderedLocusNames=SPy_0361, M5005_Spy0303;
OS Streptococcus pyogenes serotype M1.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX PubMed=11296296; DOI=10.1073/pnas.071559398;
RA Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA Clifton S.W., Roe B.A., McLaughlin R.E.;
RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX PubMed=16088826; DOI=10.1086/432514;
RA Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA Musser J.M.;
RT "Evolutionary origin and emergence of a highly successful clone of serotype
RT M1 group A Streptococcus involved multiple horizontal gene transfer
RT events.";
RL J. Infect. Dis. 192:771-782(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH
RP (4S)-4-(2-NAPHTHYLMETHYL)-D-GLUTAMIC ACID, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=17658548; DOI=10.1016/j.jmb.2007.05.003;
RA Kim K.H., Bong Y.J., Park J.K., Shin K.J., Hwang K.Y., Kim E.E.;
RT "Structural basis for glutamate racemase inhibition.";
RL J. Mol. Biol. 372:434-443(2007).
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:17658548};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00258}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17658548}.
CC -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family.
CC {ECO:0000255|HAMAP-Rule:MF_00258}.
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DR EMBL; AE004092; AAK33406.1; -; Genomic_DNA.
DR EMBL; CP000017; AAZ50922.1; -; Genomic_DNA.
DR RefSeq; NP_268685.1; NC_002737.2.
DR PDB; 2OHG; X-ray; 2.50 A; A=1-264.
DR PDB; 2OHO; X-ray; 2.25 A; A/B=1-264.
DR PDB; 2OHV; X-ray; 2.50 A; A=1-264.
DR PDBsum; 2OHG; -.
DR PDBsum; 2OHO; -.
DR PDBsum; 2OHV; -.
DR AlphaFoldDB; Q9A1B7; -.
DR SMR; Q9A1B7; -.
DR STRING; 1314.HKU360_00339; -.
DR DrugBank; DB08272; (4S)-4-(2-NAPHTHYLMETHYL)-D-GLUTAMIC ACID.
DR PaxDb; Q9A1B7; -.
DR EnsemblBacteria; AAK33406; AAK33406; SPy_0361.
DR KEGG; spy:SPy_0361; -.
DR KEGG; spz:M5005_Spy0303; -.
DR PATRIC; fig|160490.10.peg.312; -.
DR HOGENOM; CLU_052344_0_2_9; -.
DR OMA; MPWGPRT; -.
DR BRENDA; 5.1.1.3; 5935.
DR SABIO-RK; Q9A1B7; -.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; Q9A1B7; -.
DR Proteomes; UP000000750; 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; 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; 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..264
FT /note="Glutamate racemase"
FT /id="PRO_0000095521"
FT ACT_SITE 73
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O58403, ECO:0000255|HAMAP-
FT Rule:MF_00258"
FT ACT_SITE 183
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O58403, ECO:0000255|HAMAP-
FT Rule:MF_00258"
FT BINDING 10..11
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258,
FT ECO:0000305|PubMed:17658548"
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:0000255|HAMAP-Rule:MF_00258,
FT ECO:0000305|PubMed:17658548"
FT BINDING 184..185
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22634, ECO:0000255|HAMAP-
FT Rule:MF_00258"
FT STRAND 6..13
FT /evidence="ECO:0007829|PDB:2OHO"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:2OHO"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:2OHO"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:2OHO"
FT HELIX 47..62
FT /evidence="ECO:0007829|PDB:2OHO"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:2OHO"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:2OHO"
FT HELIX 74..87
FT /evidence="ECO:0007829|PDB:2OHO"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:2OHO"
FT HELIX 96..106
FT /evidence="ECO:0007829|PDB:2OHO"
FT STRAND 108..116
FT /evidence="ECO:0007829|PDB:2OHO"
FT HELIX 118..123
FT /evidence="ECO:0007829|PDB:2OHO"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:2OHO"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:2OHO"
FT HELIX 147..151
FT /evidence="ECO:0007829|PDB:2OHO"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:2OHO"
FT HELIX 159..169
FT /evidence="ECO:0007829|PDB:2OHO"
FT TURN 170..174
FT /evidence="ECO:0007829|PDB:2OHO"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:2OHO"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:2OHO"
FT HELIX 190..197
FT /evidence="ECO:0007829|PDB:2OHO"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:2OHO"
FT HELIX 206..220
FT /evidence="ECO:0007829|PDB:2OHO"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:2OHO"
FT HELIX 242..252
FT /evidence="ECO:0007829|PDB:2OHO"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:2OHO"
SQ SEQUENCE 264 AA; 29016 MW; BD7A535F8B532274 CRC64;
MDTRPIGFLD SGVGGLTVVC ELIRQLPHEK IVYIGDSARA PYGPRPKKQI KEYTWELVNF
LLTQNVKMIV FACNTATAVA WEEVKAALDI PVLGVVLPGA SAAIKSTTKG QVGVIGTPMT
VASDIYRKKI QLLAPSIQVR SLACPKFVPI VESNEMCSSI AKKIVYDSLA PLVGKIDTLV
LGCTHYPLLR PIIQNVMGPS VKLIDSGAEC VRDISVLLNY FDINGNYHQK AVEHRFFTTA
NPEIFQEIAS IWLKQKINVE HVTL
