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MURI_VIBCH
ID   MURI_VIBCH              Reviewed;         265 AA.
AC   Q9KVI7;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 116.
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=VC_0158;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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; AE003852; AAF93334.1; -; Genomic_DNA.
DR   PIR; C82358; C82358.
DR   RefSeq; NP_229815.1; NC_002505.1.
DR   RefSeq; WP_000098149.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KVI7; -.
DR   SMR; Q9KVI7; -.
DR   STRING; 243277.VC_0158; -.
DR   DNASU; 2614887; -.
DR   EnsemblBacteria; AAF93334; AAF93334; VC_0158.
DR   GeneID; 57741349; -.
DR   KEGG; vch:VC_0158; -.
DR   PATRIC; fig|243277.26.peg.145; -.
DR   eggNOG; COG0796; Bacteria.
DR   HOGENOM; CLU_052344_2_0_6; -.
DR   OMA; MPWGPRT; -.
DR   BioCyc; VCHO:VC0158-MON; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0047661; F:amino-acid racemase activity; IBA:GO_Central.
DR   GO; GO:0008881; F:glutamate racemase activity; IBA:GO_Central.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IBA:GO_Central.
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..265
FT                   /note="Glutamate racemase"
FT                   /id="PRO_0000095530"
FT   ACT_SITE        77
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   ACT_SITE        185
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         13..14
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         45..46
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         78..79
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   BINDING         186..187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
SQ   SEQUENCE   265 AA;  29196 MW;  83BAE097342673C4 CRC64;
     MSSPSFPRVL IFDSGVGGLS VYREIEARLP QLNYIYLFDN AAYPYGELTQ ETLIARVDTL
     VTRMVEQERI DLVVIACNTA STIVLPVLRA KLTIPVVGVV PAIKPASLIA SKAIGLIATP
     ATVKRQYTQE LIRDFSANKN VELLGSTRLV NMAEEKLRGK PLDLEELASI LQPLKNTIDV
     AVLGCTHFPL IKEEIQQVLG EQVQLIDSGL AIARRVQELL GIEQAVGAKQ KHRIYASAPP
     WEESALNIKL EQLGFNPVQP FLHPI
 
 
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