MURI_BRUAB
ID MURI_BRUAB Reviewed; 277 AA.
AC Q57CU6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=BruAb1_1200;
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=262698;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9-941;
RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison to
RT the highly similar genomes of Brucella melitensis and Brucella suis.";
RL J. Bacteriol. 187:2715-2726(2005).
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; AE017223; AAX74538.1; -; Genomic_DNA.
DR RefSeq; WP_002964323.1; NC_006932.1.
DR AlphaFoldDB; Q57CU6; -.
DR SMR; Q57CU6; -.
DR EnsemblBacteria; AAX74538; AAX74538; BruAb1_1200.
DR GeneID; 45052231; -.
DR GeneID; 55590871; -.
DR KEGG; bmb:BruAb1_1200; -.
DR HOGENOM; CLU_052344_2_0_5; -.
DR OMA; MPWGPRT; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000540; Chromosome I.
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.
FT CHAIN 1..277
FT /note="Glutamate racemase"
FT /id="PRO_1000047550"
FT ACT_SITE 89
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 25..26
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 57..58
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 90..91
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"
SQ SEQUENCE 277 AA; 30708 MW; B946C8EA5DD039E6 CRC64;
MKKAPAGSFP AKPTIAPERP ILVFDSGIGG LTVLREARVV MPDRRFVYIA DDAGFPYGNW
EEEALKRRII ELFGEFIANY DPEIAVIACN TASTLVLEDL RRAYPSVPFV GTVPAIKPAA
ERTSSGLVSV LATPGTVKRA YTRDLIQSFA SRCHVRLVGA DGLAAIAEAH IRGESFDEAL
VMAQIAPCFI EKDGKRTDIV VLACTHYPFL VNVLRRLAPW PVDWLDPAEA IARRMKSLLP
ARSDDDEFHS QDDLAFFTSR KPDYAIRRLM QGFGLRF
