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Database: UniProt
Entry: A0A0R1YYE8_9LACO
LinkDB: A0A0R1YYE8_9LACO
Original site: A0A0R1YYE8_9LACO 
ID   A0A0R1YYE8_9LACO        Unreviewed;       265 AA.
AC   A0A0R1YYE8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Glutamate racemase {ECO:0000256|ARBA:ARBA00013090, ECO:0000256|HAMAP-Rule:MF_00258};
DE            EC=5.1.1.3 {ECO:0000256|ARBA:ARBA00013090, ECO:0000256|HAMAP-Rule:MF_00258};
GN   Name=murI {ECO:0000256|HAMAP-Rule:MF_00258};
GN   ORFNames=FC51_GL000165 {ECO:0000313|EMBL:KRM47687.1};
OS   Lentilactobacillus parabuchneri DSM 5707 = NBRC 107865.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lentilactobacillus.
OX   NCBI_TaxID=1423784 {ECO:0000313|EMBL:KRM47687.1, ECO:0000313|Proteomes:UP000051957};
RN   [1] {ECO:0000313|EMBL:KRM47687.1, ECO:0000313|Proteomes:UP000051957}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5707 {ECO:0000313|EMBL:KRM47687.1,
RC   ECO:0000313|Proteomes:UP000051957};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
CC   -!- FUNCTION: Provides the (R)-glutamate required for cell wall
CC       biosynthesis. {ECO:0000256|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:0000256|ARBA:ARBA00001602, ECO:0000256|HAMAP-
CC         Rule:MF_00258};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00258}.
CC   -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family.
CC       {ECO:0000256|HAMAP-Rule:MF_00258}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRM47687.1}.
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DR   EMBL; AZGK01000001; KRM47687.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R1YYE8; -.
DR   PATRIC; fig|1423784.4.peg.164; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000051957; Unassembled WGS sequence.
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   Gene3D; 3.40.50.1860; -; 2.
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   NCBIfam; TIGR00067; glut_race; 1.
DR   PANTHER; PTHR21198; GLUTAMATE RACEMASE; 1.
DR   PANTHER; PTHR21198:SF2; GLUTAMATE RACEMASE; 1.
DR   Pfam; PF01177; Asp_Glu_race; 1.
DR   SUPFAM; SSF53681; Aspartate/glutamate racemase; 2.
DR   PROSITE; PS00923; ASP_GLU_RACEMASE_1; 1.
DR   PROSITE; PS00924; ASP_GLU_RACEMASE_2; 1.
PE   3: Inferred from homology;
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00258};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00258};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00258};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00258}.
FT   ACT_SITE        73
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   ACT_SITE        184
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         10..11
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         42..43
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         74..75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         185..186
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
SQ   SEQUENCE   265 AA;  28546 MW;  45E760C9EE5AF3B4 CRC64;
     MDKRPIGVMD SGVGGLTVLK EITKVLPNES YIFVGDQANL PYGQKSSEVV RALTKRIADY
     MLAQDVKMFV IACNTATAAA YEYLTKILPI PVIGVIQPGA TSAANVSKTG QIGVIATNGT
     VRSGDYQRLI KQANPHAKVS SLGCPEFVTM VEEGLAGTVE AQAAVNNRLA WFMDKPIDTL
     VMGCTHFPVL RTEIQNVVGP DVTLVDPGIA TAQQVLDYLQ QHDALNDRSA SRQTREYFTT
     GKPKDFAKIA DQLLGEPISA AHLDI
//
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