MURI_SALTY
ID MURI_SALTY Reviewed; 283 AA.
AC P40723;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 140.
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=STM4131;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-46.
RX PubMed=1448622; DOI=10.1016/0923-2508(92)90091-2;
RA Wei B.Y., Bradbeer C., Kadner R.J.;
RT "Conserved structural and regulatory regions in the Salmonella typhimurium
RT btuB gene for the outer membrane vitamin B12 transport protein.";
RL Res. Microbiol. 143:459-466(1992).
RN [3]
RP IDENTIFICATION.
RX PubMed=7920643; DOI=10.1038/ng0694-205;
RA Robison K., Gilbert W., Church G.M.;
RT "Large scale bacterial gene discovery by similarity search.";
RL Nat. Genet. 7:205-214(1994).
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; AE006468; AAL22969.1; -; Genomic_DNA.
DR EMBL; M89481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_463010.1; NC_003197.2.
DR RefSeq; WP_000201805.1; NC_003197.2.
DR AlphaFoldDB; P40723; -.
DR SMR; P40723; -.
DR STRING; 99287.STM4131; -.
DR PaxDb; P40723; -.
DR EnsemblBacteria; AAL22969; AAL22969; STM4131.
DR GeneID; 1255657; -.
DR KEGG; stm:STM4131; -.
DR PATRIC; fig|99287.12.peg.4352; -.
DR HOGENOM; CLU_052344_2_0_6; -.
DR OMA; MPWGPRT; -.
DR PhylomeDB; P40723; -.
DR BioCyc; SENT99287:STM4131-MON; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0047661; F:amino-acid racemase activity; IBA:GO_Central.
DR GO; GO:0008881; F:glutamate racemase activity; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..283
FT /note="Glutamate racemase"
FT /id="PRO_0000095504"
FT ACT_SITE 92
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT ACT_SITE 204
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 28..29
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 60..61
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 93..94
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 205..206
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT CONFLICT 41..45
FT /note="RRLLP -> SAAPA (in Ref. 2; M89481)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 283 AA; 31043 MW; A2DBB2D8A76C4C84 CRC64;
MATKLQDENT PCLAATPSEP RPTVLVFDSG VGGLSVYDEI RRLLPDLHYI YAFDNVAFPY
GEKSETFIVE RVVEIVTAVQ QRYPLSLAVI ACNTASTVSL PALREKFAFP VVGVVPAIKP
AARLTANGVV GLLATRATVK RPYTHELIAR FANECQIAML GSAELVELAE AKLHGDSVSL
EELRRILRPW LRMPEPPDTV VLGCTHFPLL RDELLQVLPE GTRLVDSGAA IARRTAWLLE
HEAPDAKSTD ANIAYCMAMT PGAEQLLPVL QRYGFETLEK LPV
