MURI_EXIS2
ID MURI_EXIS2 Reviewed; 271 AA.
AC B1YJW7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=Exig_2153;
OS Exiguobacterium sibiricum (strain DSM 17290 / CIP 109462 / JCM 13490 /
OS 255-15).
OC Bacteria; Firmicutes; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX NCBI_TaxID=262543;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C.,
RA Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T.,
RA Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Exiguobacterium sibiricum 255-15.";
RL Submitted (APR-2008) 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; CP001022; ACB61605.1; -; Genomic_DNA.
DR RefSeq; WP_012371022.1; NC_010556.1.
DR AlphaFoldDB; B1YJW7; -.
DR SMR; B1YJW7; -.
DR STRING; 262543.Exig_2153; -.
DR EnsemblBacteria; ACB61605; ACB61605; Exig_2153.
DR KEGG; esi:Exig_2153; -.
DR eggNOG; COG0796; Bacteria.
DR HOGENOM; CLU_052344_0_2_9; -.
DR OMA; MPWGPRT; -.
DR OrthoDB; 1718671at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001681; 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; 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..271
FT /note="Glutamate racemase"
FT /id="PRO_1000114044"
FT ACT_SITE 72
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT ACT_SITE 183
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 9..10
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 41..42
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 73..74
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 184..185
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
SQ SEQUENCE 271 AA; 29751 MW; 1EE927F1399EB973 CRC64;
MNRSIGVLDS GVGGLTVARE LMRQLPHEQI IYVGDTLRCP YGPRPEEEIR QFTWEMIDFL
VAQGVKLIVI ACNTATAVVL KEARQKLSIP VIGVIDPGAR AAVKVTRSKR IGVIGTKMTI
ESNSYEKALR HVEGQVVVES LSCPPFVPLV ESSQTSGPYV ERVVANTLKP LLSYDMDTLI
LGCTHYPLLA EVIGRVIGPN VQLISSGDET ALEVSALLDY NGITADLDRI PEHVYHATGD
TRSFERIASD WLHHPVQAKR LVLGTEEEKC V