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Database: UniProt
Entry: A0A1H3JUW2_9CLOT
LinkDB: A0A1H3JUW2_9CLOT
Original site: A0A1H3JUW2_9CLOT 
ID   A0A1H3JUW2_9CLOT        Unreviewed;       283 AA.
AC   A0A1H3JUW2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=SAMN05192546_102121 {ECO:0000313|EMBL:SDY43747.1};
OS   Tindallia californiensis.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Tindallia.
OX   NCBI_TaxID=159292 {ECO:0000313|EMBL:SDY43747.1, ECO:0000313|Proteomes:UP000199230};
RN   [1] {ECO:0000313|EMBL:SDY43747.1, ECO:0000313|Proteomes:UP000199230}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APO {ECO:0000313|EMBL:SDY43747.1,
RC   ECO:0000313|Proteomes:UP000199230};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; FNPV01000002; SDY43747.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3JUW2; -.
DR   STRING; 159292.SAMN05192546_102121; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000199230; 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; IPR004391; Glu_race.
DR   NCBIfam; TIGR00067; glut_race; 1.
DR   PANTHER; PTHR21198; GLUTAMATE RACEMASE; 1.
DR   PANTHER; PTHR21198:SF3; 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.
PE   3: Inferred from homology;
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW   Rule:MF_00258};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_00258};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00258};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW   Rule:MF_00258}; Reference proteome {ECO:0000313|Proteomes:UP000199230}.
FT   ACT_SITE        76
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   ACT_SITE        186
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         13..14
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         45..46
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         77..78
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
FT   BINDING         187..188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00258"
SQ   SEQUENCE   283 AA;  30982 MW;  59FBF440C3A1E650 CRC64;
     MEEVNQGPIG VFDSGYGGIS VLANLIEAMP KESFVYISDS INAPYGELES QEVLNHALNH
     MRILEKQSAK AVVIACNTAT SAAATALRAK YSFPIIGMEP AVKPAITKSS SGKILVAATG
     LTLKERKFAA LVKKMDLQHN IVTLPCHGLV EIIEEYGPES KEVTKKLDEL LAPLQPLNVD
     GVVLGCTHYV LIKNQWKAAL PEGTRIHDGN EGTVKQTMRM IMENTTITKA HSMGKVSLMD
     SSQDDERLEK SKQLLQNQLR INGIVSSDQL EIELRKNNEL CKS
//
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