MURI_STAAR
ID MURI_STAAR Reviewed; 266 AA.
AC Q6GHT5;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
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};
GN Name=murI {ECO:0000255|HAMAP-Rule:MF_00258}; OrderedLocusNames=SAR1123;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, 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).
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};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00258}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17568739}.
CC -!- INTERACTION:
CC Q6GHT5; Q6GHT5: murI; NbExp=4; IntAct=EBI-15642790, EBI-15642790;
CC -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family.
CC {ECO:0000255|HAMAP-Rule:MF_00258}.
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DR EMBL; BX571856; CAG40126.1; -; Genomic_DNA.
DR RefSeq; WP_001039660.1; NC_002952.2.
DR PDB; 2JFQ; X-ray; 2.15 A; A/B=1-266.
DR PDBsum; 2JFQ; -.
DR AlphaFoldDB; Q6GHT5; -.
DR SMR; Q6GHT5; -.
DR DIP; DIP-60302N; -.
DR KEGG; sar:SAR1123; -.
DR HOGENOM; CLU_052344_0_2_9; -.
DR OMA; MPWGPRT; -.
DR OrthoDB; 1718671at2; -.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; Q6GHT5; -.
DR Proteomes; UP000000596; 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..266
FT /note="Glutamate racemase"
FT /id="PRO_0000095510"
FT ACT_SITE 72
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O58403, ECO:0000255|HAMAP-
FT Rule:MF_00258"
FT ACT_SITE 184
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O58403, ECO:0000255|HAMAP-
FT Rule:MF_00258"
FT BINDING 9..10
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258,
FT ECO:0000269|PubMed:17568739, ECO:0007744|PDB:2JFQ"
FT BINDING 41..42
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258,
FT ECO:0000269|PubMed:17568739, ECO:0007744|PDB:2JFQ"
FT BINDING 73..74
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258,
FT ECO:0000269|PubMed:17568739, ECO:0007744|PDB:2JFQ"
FT BINDING 185..186
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258,
FT ECO:0000269|PubMed:17568739, ECO:0007744|PDB:2JFQ"
FT STRAND 5..12
FT /evidence="ECO:0007829|PDB:2JFQ"
FT HELIX 15..24
FT /evidence="ECO:0007829|PDB:2JFQ"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:2JFQ"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:2JFQ"
FT HELIX 46..60
FT /evidence="ECO:0007829|PDB:2JFQ"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:2JFQ"
FT HELIX 73..86
FT /evidence="ECO:0007829|PDB:2JFQ"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:2JFQ"
FT HELIX 95..105
FT /evidence="ECO:0007829|PDB:2JFQ"
FT STRAND 107..115
FT /evidence="ECO:0007829|PDB:2JFQ"
FT HELIX 117..122
FT /evidence="ECO:0007829|PDB:2JFQ"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:2JFQ"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:2JFQ"
FT HELIX 146..151
FT /evidence="ECO:0007829|PDB:2JFQ"
FT HELIX 158..169
FT /evidence="ECO:0007829|PDB:2JFQ"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:2JFQ"
FT STRAND 178..186
FT /evidence="ECO:0007829|PDB:2JFQ"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:2JFQ"
FT HELIX 191..197
FT /evidence="ECO:0007829|PDB:2JFQ"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:2JFQ"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:2JFQ"
FT HELIX 207..221
FT /evidence="ECO:0007829|PDB:2JFQ"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:2JFQ"
FT HELIX 243..253
FT /evidence="ECO:0007829|PDB:2JFQ"
SQ SEQUENCE 266 AA; 29702 MW; 97FC71DB4A2C7B0E CRC64;
MNKPIGVIDS GVGGLTVAKE IMRQLPNETI YYLGDIGRCP YGPRPGEQVK QYTVEIARKL
MEFDIKMLVI ACNTATAVAL EYLQKTLSIP VIGVIEPGAR TAIMTTRNQN VLVLGTEGTI
KSEAYRTHIK RINPHVEVHG VACPGFVPLV EQMRYSDPTI TSIVIHQTLK RWRNSESDTV
ILGCTHYPLL YKPIYDYFGG KKTVISSGLE TAREVSALLT FSNEHASYTE HPDHRFFATG
DTTHITNIIK EWLNLSVNVE RISVND
