MURI_BIFA0
ID MURI_BIFA0 Reviewed; 258 AA.
AC B8DT03;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=BLA_0840;
OS Bifidobacterium animalis subsp. lactis (strain AD011).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=442563;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD011;
RX PubMed=19011029; DOI=10.1128/jb.01515-08;
RA Kim J.F., Jeong H., Yu D.S., Choi S.-H., Hur C.-G., Park M.-S., Yoon S.H.,
RA Kim D.-W., Ji G.E., Park H.-S., Oh T.K.;
RT "Genome sequence of the probiotic bacterium Bifidobacterium animalis subsp.
RT lactis AD011.";
RL J. Bacteriol. 191:678-679(2009).
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; CP001213; ACL29132.1; -; Genomic_DNA.
DR RefSeq; WP_004218555.1; NC_011835.1.
DR AlphaFoldDB; B8DT03; -.
DR SMR; B8DT03; -.
DR STRING; 442563.BLA_0840; -.
DR EnsemblBacteria; ACL29132; ACL29132; BLA_0840.
DR GeneID; 66533602; -.
DR KEGG; bla:BLA_0840; -.
DR HOGENOM; CLU_052344_1_0_11; -.
DR OMA; MPWGPRT; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002456; 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 TIGRFAMs; TIGR00067; glut_race; 1.
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..258
FT /note="Glutamate racemase"
FT /id="PRO_1000125601"
FT ACT_SITE 74
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT ACT_SITE 187
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 11..12
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 43..44
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 75..76
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 188..189
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
SQ SEQUENCE 258 AA; 28801 MW; 27B4B90800E14D34 CRC64;
MTSSAPVGVF DSGLGGISVV RQIRTDLPHE RILYFGDSAN APYGTKTPEQ VRDLSFRIVE
DFVEQGAKAV VIACNTATSS AVQELREHYD IPIIGMEPAL KVACDRGHGE RQSVIVAATP
LTLRERKFAA LMHRFEDAHT IHKQPCPRLV EIVERGELDD HDLVMRTLHD YFDQYDLAHT
DSVVLGCTHF VFYRDYFREL LPNNVAIVDG NEGTARHLEV VLESLGKLAP EEQDGGVILR
NSDPGERIAE LAQQLLER