MURI_ECOLI
ID MURI_ECOLI Reviewed; 285 AA.
AC P22634; P78133; Q2M8R2;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Glutamate racemase {ECO:0000255|HAMAP-Rule:MF_00258, ECO:0000303|PubMed:8098327};
DE EC=5.1.1.3 {ECO:0000255|HAMAP-Rule:MF_00258, ECO:0000269|PubMed:17568739, ECO:0000269|PubMed:8098327};
GN Name=murI {ECO:0000255|HAMAP-Rule:MF_00258, ECO:0000303|PubMed:1355768,
GN ECO:0000303|PubMed:8098327}; Synonyms=dga, glr, yijA;
GN OrderedLocusNames=b3967, JW5550;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7028991; DOI=10.1016/0022-2836(81)90508-8;
RA Brosius J., Dull T.J., Sleeter D.D., Noller H.F.;
RT "Gene organization and primary structure of a ribosomal RNA operon from
RT Escherichia coli.";
RL J. Mol. Biol. 148:107-127(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6297582; DOI=10.1016/0167-4781(83)90027-1;
RA Boros I., Csordas-Toth E., Kiss A., Kiss I., Toeroek I., Udvardy A.,
RA Udvardy K., Venetianer P.;
RT "Identification of two new promoters probably involved in the transcription
RT of a ribosomal RNA gene of Escherichia coli.";
RL Biochim. Biophys. Acta 739:173-180(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B;
RX PubMed=8093236; DOI=10.1128/jb.175.1.111-116.1993;
RA Dougherty T.J., Thanassi J.A., Pucci M.J.;
RT "The Escherichia coli mutant requiring D-glutamic acid is the result of
RT mutations in two distinct genetic loci.";
RL J. Bacteriol. 175:111-116(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP CHARACTERIZATION, PATHWAY, AND FUNCTION.
RC STRAIN=K12;
RX PubMed=1355768; DOI=10.1128/jb.174.18.5772-5779.1992;
RA Doublet P., van Heijenoort J., Mengin-Lecreulx D.;
RT "Identification of the Escherichia coli murI gene, which is required for
RT the biosynthesis of D-glutamic acid, a specific component of bacterial
RT peptidoglycan.";
RL J. Bacteriol. 174:5772-5779(1992).
RN [8]
RP CHARACTERIZATION, PATHWAY, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8098327; DOI=10.1128/jb.175.10.2970-2979.1993;
RA Doublet P., van Heijenoort J., Bohin J.-P., Mengin-Lecreulx D.;
RT "The murI gene of Escherichia coli is an essential gene that encodes a
RT glutamate racemase activity.";
RL J. Bacteriol. 175:2970-2979(1993).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH GLUTAMATE AND
RP UDP-N-ACETYL-ALPHA-D-MURAMOYL-L-ALANINE, FUNCTION, PATHWAY, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, 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 ECO:0000269|PubMed:1355768, ECO:0000269|PubMed:8098327,
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:8098327};
CC -!- ACTIVITY REGULATION: The low basal catalytic activity in increased
CC 1000-fold in the presence of UDP-MurNAc-L-Ala, the product of the
CC preceding enzyme in the peptidoglycan biosynthesis.
CC {ECO:0000269|PubMed:17568739}.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00258, ECO:0000269|PubMed:1355768,
CC ECO:0000269|PubMed:8098327, ECO:0000305|PubMed:17568739}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17568739}.
CC -!- INTERACTION:
CC P22634; P0CE47: tufA; NbExp=2; IntAct=EBI-554903, EBI-301077;
CC -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family.
CC {ECO:0000255|HAMAP-Rule:MF_00258}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA23677.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC43073.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA23637.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA23638.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; V00348; CAA23638.1; ALT_INIT; Genomic_DNA.
DR EMBL; V00347; CAA23637.1; ALT_INIT; Genomic_DNA.
DR EMBL; L14556; AAA23677.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00006; AAC43073.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76949.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77344.1; -; Genomic_DNA.
DR PIR; I41187; I41187.
DR RefSeq; NP_418402.2; NC_000913.3.
DR RefSeq; WP_000201820.1; NZ_SSZK01000065.1.
DR PDB; 2JFN; X-ray; 1.90 A; A=1-285.
DR PDBsum; 2JFN; -.
DR AlphaFoldDB; P22634; -.
DR SMR; P22634; -.
DR BioGRID; 4259606; 251.
DR BioGRID; 852763; 9.
DR DIP; DIP-10283N; -.
DR IntAct; P22634; 14.
DR STRING; 511145.b3967; -.
DR jPOST; P22634; -.
DR PaxDb; P22634; -.
DR PRIDE; P22634; -.
DR EnsemblBacteria; AAC76949; AAC76949; b3967.
DR EnsemblBacteria; BAE77344; BAE77344; BAE77344.
DR GeneID; 948467; -.
DR KEGG; ecj:JW5550; -.
DR KEGG; eco:b3967; -.
DR PATRIC; fig|1411691.4.peg.2737; -.
DR EchoBASE; EB1189; -.
DR eggNOG; COG0796; Bacteria.
DR HOGENOM; CLU_052344_2_0_6; -.
DR InParanoid; P22634; -.
DR OMA; MPWGPRT; -.
DR PhylomeDB; P22634; -.
DR BioCyc; EcoCyc:GLUTRACE-MON; -.
DR BioCyc; MetaCyc:GLUTRACE-MON; -.
DR SABIO-RK; P22634; -.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; P22634; -.
DR PRO; PR:P22634; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0047661; F:amino-acid racemase activity; IBA:GO_Central.
DR GO; GO:0008881; F:glutamate racemase activity; IDA:EcoCyc.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IMP:EcoCyc.
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; Reference proteome.
FT CHAIN 1..285
FT /note="Glutamate racemase"
FT /id="PRO_0000095470"
FT ACT_SITE 92
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O58403, ECO:0000255|HAMAP-
FT Rule:MF_00258"
FT ACT_SITE 204
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O58403, ECO:0000255|HAMAP-
FT Rule:MF_00258"
FT BINDING 28..29
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258,
FT ECO:0000269|PubMed:17568739, ECO:0007744|PDB:2JFN"
FT BINDING 60..61
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258,
FT ECO:0000269|PubMed:17568739, ECO:0007744|PDB:2JFN"
FT BINDING 93..94
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258,
FT ECO:0000269|PubMed:17568739, ECO:0007744|PDB:2JFN"
FT BINDING 104
FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanine"
FT /ligand_id="ChEBI:CHEBI:83898"
FT /evidence="ECO:0000269|PubMed:17568739,
FT ECO:0007744|PDB:2JFN"
FT BINDING 113..119
FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanine"
FT /ligand_id="ChEBI:CHEBI:83898"
FT /evidence="ECO:0000269|PubMed:17568739,
FT ECO:0007744|PDB:2JFN"
FT BINDING 205..206
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258,
FT ECO:0000269|PubMed:17568739, ECO:0007744|PDB:2JFN"
FT STRAND 21..31
FT /evidence="ECO:0007829|PDB:2JFN"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:2JFN"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:2JFN"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:2JFN"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:2JFN"
FT HELIX 65..82
FT /evidence="ECO:0007829|PDB:2JFN"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:2JFN"
FT HELIX 93..106
FT /evidence="ECO:0007829|PDB:2JFN"
FT HELIX 118..124
FT /evidence="ECO:0007829|PDB:2JFN"
FT STRAND 126..134
FT /evidence="ECO:0007829|PDB:2JFN"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:2JFN"
FT HELIX 142..150
FT /evidence="ECO:0007829|PDB:2JFN"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:2JFN"
FT HELIX 163..173
FT /evidence="ECO:0007829|PDB:2JFN"
FT HELIX 180..186
FT /evidence="ECO:0007829|PDB:2JFN"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:2JFN"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:2JFN"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:2JFN"
FT HELIX 211..217
FT /evidence="ECO:0007829|PDB:2JFN"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:2JFN"
FT HELIX 228..241
FT /evidence="ECO:0007829|PDB:2JFN"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:2JFN"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:2JFN"
FT HELIX 267..272
FT /evidence="ECO:0007829|PDB:2JFN"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:2JFN"
SQ SEQUENCE 285 AA; 31002 MW; EC87281B577B8E93 CRC64;
MATKLQDGNT PCLAATPSEP RPTVLVFDSG VGGLSVYDEI RHLLPDLHYI YAFDNVAFPY
GEKSEAFIVE RVVAIVTAVQ ERYPLALAVV ACNTASTVSL PALREKFDFP VVGVVPAIKP
AARLTANGIV GLLATRGTVK RSYTHELIAR FANECQIEML GSAEMVELAE AKLHGEDVSL
DALKRILRPW LRMKEPPDTV VLGCTHFPLL QEELLQVLPE GTRLVDSGAA IARRTAWLLE
HEAPDAKSAD ANIAFCMAMT PGAEQLLPVL QRYGFETLEK LAVLG
