MURI_RUEST
ID MURI_RUEST Reviewed; 269 AA.
AC Q1GHL1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=TM1040_1122;
OS Ruegeria sp. (strain TM1040) (Silicibacter sp.).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria; unclassified Ruegeria.
OX NCBI_TaxID=292414;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM1040;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Goodwin L., Thompson L.S.,
RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Belas R., Moran M.A., Buchan A., Gonzalez J.M., Schell M.A., Sun F.,
RA Richardson P.;
RT "Complete sequence of chromosome of Silicibacter sp. TM1040.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000377; ABF63855.1; -; Genomic_DNA.
DR RefSeq; WP_011538462.1; NC_008044.1.
DR AlphaFoldDB; Q1GHL1; -.
DR SMR; Q1GHL1; -.
DR STRING; 292414.TM1040_1122; -.
DR EnsemblBacteria; ABF63855; ABF63855; TM1040_1122.
DR KEGG; sit:TM1040_1122; -.
DR eggNOG; COG0796; Bacteria.
DR HOGENOM; CLU_052344_0_3_5; -.
DR OMA; LDFFKPH; -.
DR OrthoDB; 1718671at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000636; Chromosome.
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; IPR004391; Glu_race.
DR PANTHER; PTHR21198:SF2; PTHR21198:SF2; 1.
DR Pfam; PF01177; Asp_Glu_race; 1.
DR SUPFAM; SSF53681; SSF53681; 2.
DR PROSITE; PS00923; ASP_GLU_RACEMASE_1; 1.
PE 3: Inferred from homology;
KW Cell shape; Cell wall biogenesis/degradation; Isomerase;
KW Peptidoglycan synthesis; Reference proteome.
FT CHAIN 1..269
FT /note="Glutamate racemase"
FT /id="PRO_1000078575"
FT ACT_SITE 70
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT ACT_SITE 194
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 7..8
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 39..40
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 71..72
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 195..196
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
SQ SEQUENCE 269 AA; 29177 MW; 9CD62A40F6B9023F CRC64;
MAVGIFDSGL GGLTVLDAAQ KRLPDVDFLY YGDNSHAPYG VRDAEDIYEL THKAVHDMWD
RGCNLVILAC NTASAAALRR MQEAGVPEGK RVLGVFVPLI EALTERQWGD NSPPREVAVK
HVALFATPAT VASRAFQREL AFRAIGVDVE AQACGGVVDA IEEGDMILAE ALVKSHVDAL
LRKMPRPEAA ILGCTHYPLM EDVFQKALGP DVQVFSQGRL VADSLAHYLE RRPEMIGGGN
AGYVTTGNAN RVSSRATQFL RREITFEAA