MURI_PSEA8
ID MURI_PSEA8 Reviewed; 265 AA.
AC B7V0K8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Glutamate racemase {ECO:0000255|HAMAP-Rule:MF_00258};
DE EC=5.1.1.3 {ECO:0000255|HAMAP-Rule:MF_00258};
GN Name=murI {ECO:0000255|HAMAP-Rule:MF_00258}; OrderedLocusNames=PLES_50481;
OS Pseudomonas aeruginosa (strain LESB58).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=557722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LESB58;
RX PubMed=19047519; DOI=10.1101/gr.086082.108;
RA Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I.,
RA Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L., Quail M.A.,
RA Lennard N., Bignell A., Clarke L., Seeger K., Saunders D., Harris D.,
RA Parkhill J., Hancock R.E.W., Brinkman F.S.L., Levesque R.C.;
RT "Newly introduced genomic prophage islands are critical determinants of in
RT vivo competitiveness in the Liverpool epidemic strain of Pseudomonas
RT aeruginosa.";
RL Genome Res. 19:12-23(2009).
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 -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00258}.
CC -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family.
CC {ECO:0000255|HAMAP-Rule:MF_00258}.
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DR EMBL; FM209186; CAW29802.1; -; Genomic_DNA.
DR RefSeq; WP_003099300.1; NC_011770.1.
DR AlphaFoldDB; B7V0K8; -.
DR SMR; B7V0K8; -.
DR KEGG; pag:PLES_50481; -.
DR HOGENOM; CLU_052344_1_0_6; -.
DR OMA; MPWGPRT; -.
DR UniPathway; UPA00219; -.
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 3: Inferred from homology;
KW Cell shape; Cell wall biogenesis/degradation; Isomerase;
KW Peptidoglycan synthesis.
FT CHAIN 1..265
FT /note="Glutamate racemase"
FT /id="PRO_1000119190"
FT ACT_SITE 75
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT ACT_SITE 186
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 12..13
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 44..45
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 76..77
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 187..188
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
SQ SEQUENCE 265 AA; 28275 MW; B60E3D836A739CD7 CRC64;
MAVESAAVGV FDSGVGGLSV LREIRARLPS ESLLYVADNA HVPYGEKSAE YIRERCERIG
DFLLEQGAKA LVLACNTATA AAAAELRERY PQVPLVAMEP AVKPAAAATR NGRVGVLATT
GTLKSARFAA LLDRFASDVQ VFTQPCPGLV ERIEAGDLYG PQTRALLERL LAPILEQGCD
TLILGCTHYP FVKPLLAELI PAEMAVIDTG AAVARQLERV LSARALLASG QAATPRFWTS
ALPEEMERIL PILWGSPESV GKLVV
