MURI_SULSY
ID MURI_SULSY Reviewed; 260 AA.
AC B2V9I5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 86.
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};
GN OrderedLocusNames=SYO3AOP1_0987;
OS Sulfurihydrogenibium sp. (strain YO3AOP1).
OC Bacteria; Aquificae; Aquificales; Hydrogenothermaceae;
OC Sulfurihydrogenibium; unclassified Sulfurihydrogenibium.
OX NCBI_TaxID=436114;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YO3AOP1;
RX PubMed=19136599; DOI=10.1128/jb.01645-08;
RA Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT "Complete and draft genome sequences of six members of the Aquificales.";
RL J. Bacteriol. 191:1992-1993(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001080; ACD66608.1; -; Genomic_DNA.
DR RefSeq; WP_012459678.1; NC_010730.1.
DR AlphaFoldDB; B2V9I5; -.
DR SMR; B2V9I5; -.
DR STRING; 436114.SYO3AOP1_0987; -.
DR EnsemblBacteria; ACD66608; ACD66608; SYO3AOP1_0987.
DR KEGG; sul:SYO3AOP1_0987; -.
DR eggNOG; COG0796; Bacteria.
DR HOGENOM; CLU_052344_0_2_0; -.
DR OMA; MPWGPRT; -.
DR OrthoDB; 1718671at2; -.
DR UniPathway; UPA00219; -.
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..260
FT /note="Glutamate racemase"
FT /id="PRO_1000114069"
FT ACT_SITE 71
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT ACT_SITE 182
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 7..8
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 39..40
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 72..73
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 183..184
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
SQ SEQUENCE 260 AA; 28723 MW; 3CEA7E3B90B1920A CRC64;
MPIGIFDSGI GGLTVFKEIA ASFPKVDLYY LGDTARVPYG NKSKTTIIRY SVECASYLYH
NYNVDAIVIA CNTASSYALD TLREILPIPV IGVVQPGAES AVKVSKNKKI GVIGTSATIK
SNSYFETLKS LDKDLEIYQK ACPLFVPLVE EGWIDNEVAK LTVKEYLDDL VKTGIDTLIL
GCTHYPLLKN TIKGLYPHLN IVDSSVAIVE HLKNIKLNIE ETGKRKIFIT DESHAFDKLK
NMLVGDIKTE KIELSDLCSL
