MURI_CAMFF
ID MURI_CAMFF Reviewed; 253 AA.
AC A0RNJ6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=CFF8240_0590;
OS Campylobacter fetus subsp. fetus (strain 82-40).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=82-40;
RA Fouts D.E., Nelson K.E.;
RT "Sequence of Campylobacter fetus subsp. fetus 82-40.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000487; ABK82704.1; -; Genomic_DNA.
DR RefSeq; WP_002849001.1; NC_008599.1.
DR AlphaFoldDB; A0RNJ6; -.
DR SMR; A0RNJ6; -.
DR STRING; 360106.CFF8240_0590; -.
DR EnsemblBacteria; ABK82704; ABK82704; CFF8240_0590.
DR GeneID; 61064435; -.
DR KEGG; cff:CFF8240_0590; -.
DR eggNOG; COG0796; Bacteria.
DR HOGENOM; CLU_052344_1_0_7; -.
DR OMA; LDFFKPH; -.
DR OrthoDB; 1718671at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000760; 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 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.
FT CHAIN 1..253
FT /note="Glutamate racemase"
FT /id="PRO_1000047554"
FT ACT_SITE 70
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT ACT_SITE 178
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 71..72
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT BINDING 179..180
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
SQ SEQUENCE 253 AA; 27969 MW; 9290CC54DA5018AC CRC64;
MKIAIFDSGI GGLSLLNEAL KRFRGVEFIY FADNKNAPYG TKSKDEIIRL CLNCVQFLTN
LSVDMIVIAC NTATSAAITE LRSSFSVPII GMEPAVKLGV NAGGDILVVA TPATISGNKL
SDLIHKVNLE SKTHLLALPK LVEFAQNMEF DSLEVLKYLK DEISKFDLSN ISLLVLGCTH
FNYFKDSFRA ILPNKTGIID GVNGTINQMI RRLGGVSEFG DKNSIRYISS TENLNVKKIE
PYLKRLDIMR EIN