MURI_LISMO
ID MURI_LISMO Reviewed; 266 AA.
AC Q8Y7N7;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 119.
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}; Synonyms=racE;
GN OrderedLocusNames=lmo1237;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH SUCCINATE.
RA Majorek K.A., Chruszcz M., Skarina T., Onopriyenko O., Stam J.,
RA Anderson W.F., Savchenko A., Bujnicki J.M., Minor W.;
RT "Crystal structure of glutamate racemase from Listeria monocytogenes in
RT complex with succinic acid.";
RL Submitted (AUG-2009) to the PDB data bank.
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; AL591978; CAC99315.1; -; Genomic_DNA.
DR PIR; AE1229; AE1229.
DR RefSeq; NP_464762.1; NC_003210.1.
DR RefSeq; WP_003723856.1; NZ_CP023861.1.
DR PDB; 3HFR; X-ray; 2.30 A; A/B=1-266.
DR PDB; 3IST; X-ray; 1.65 A; A/B=1-266.
DR PDB; 3ISV; X-ray; 1.85 A; A/B=1-266.
DR PDBsum; 3HFR; -.
DR PDBsum; 3IST; -.
DR PDBsum; 3ISV; -.
DR AlphaFoldDB; Q8Y7N7; -.
DR SMR; Q8Y7N7; -.
DR STRING; 169963.lmo1237; -.
DR DrugBank; DB02343; 3,6,9,12,15-Pentaoxaheptadecane.
DR PaxDb; Q8Y7N7; -.
DR EnsemblBacteria; CAC99315; CAC99315; CAC99315.
DR GeneID; 986027; -.
DR KEGG; lmo:lmo1237; -.
DR PATRIC; fig|169963.11.peg.1269; -.
DR eggNOG; COG0796; Bacteria.
DR HOGENOM; CLU_052344_0_2_9; -.
DR OMA; MPWGPRT; -.
DR PhylomeDB; Q8Y7N7; -.
DR BioCyc; LMON169963:LMO1237-MON; -.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; Q8Y7N7; -.
DR Proteomes; UP000000817; 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 1: Evidence at protein level;
KW 3D-structure; Cell shape; Cell wall biogenesis/degradation; Isomerase;
KW Peptidoglycan synthesis; Reference proteome.
FT CHAIN 1..266
FT /note="Glutamate racemase"
FT /id="PRO_0000095487"
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 183
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:0000250|UniProtKB:P22634, ECO:0000255|HAMAP-
FT Rule:MF_00258"
FT BINDING 41..42
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22634, ECO:0000255|HAMAP-
FT Rule:MF_00258, ECO:0007744|PDB:3IST"
FT BINDING 73..74
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22634, ECO:0000255|HAMAP-
FT Rule:MF_00258"
FT BINDING 184..185
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22634, ECO:0000255|HAMAP-
FT Rule:MF_00258"
FT STRAND 5..12
FT /evidence="ECO:0007829|PDB:3IST"
FT HELIX 15..24
FT /evidence="ECO:0007829|PDB:3IST"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:3IST"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:3IST"
FT HELIX 46..62
FT /evidence="ECO:0007829|PDB:3IST"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:3IST"
FT HELIX 73..86
FT /evidence="ECO:0007829|PDB:3IST"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:3IST"
FT HELIX 95..105
FT /evidence="ECO:0007829|PDB:3IST"
FT STRAND 107..115
FT /evidence="ECO:0007829|PDB:3IST"
FT HELIX 117..122
FT /evidence="ECO:0007829|PDB:3IST"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:3IST"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:3IST"
FT HELIX 145..151
FT /evidence="ECO:0007829|PDB:3IST"
FT HELIX 158..168
FT /evidence="ECO:0007829|PDB:3IST"
FT HELIX 169..173
FT /evidence="ECO:0007829|PDB:3IST"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:3IST"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:3IST"
FT HELIX 190..197
FT /evidence="ECO:0007829|PDB:3IST"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:3IST"
FT HELIX 207..220
FT /evidence="ECO:0007829|PDB:3IST"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:3IST"
FT HELIX 241..252
FT /evidence="ECO:0007829|PDB:3IST"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:3IST"
SQ SEQUENCE 266 AA; 29160 MW; 912A19482409991B CRC64;
MKQAIGFIDS GVGGLTVVRE VLKQLPHEQV YYLGDTARCP YGPRDKEEVA KFTWEMTNFL
VDRGIKMLVI ACNTATAAAL YDIREKLDIP VIGVIQPGSR AALKATRNNK IGVLGTLGTV
ESMAYPTALK GLNRRVEVDS LACPKFVSVV ESGEYKSAIA KKVVAESLLP LKSTKIDTVI
LGCTHYPLLK PIIENFMGDG VAVINSGEET ASEVSALLDY HNLLDATDEE IEHRFFTTGS
TQIFKDIAKD WLNMPDMTVE HIKLGK
