(data stored in ACNUC9435 zone)

SWISSPROT: MURI_LISIN

ID   MURI_LISIN              Reviewed;         266 AA.
AC   Q92CH2;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   11-DEC-2019, entry version 102.
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}; Synonyms=racE;
GN   OrderedLocusNames=lin1200;
OS   Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=272626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-680 / CLIP 11262;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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}.
DR   EMBL; AL596167; CAC96431.1; -; Genomic_DNA.
DR   PIR; AG1582; AG1582.
DR   RefSeq; WP_003761886.1; NC_003212.1.
DR   SMR; Q92CH2; -.
DR   STRING; 272626.lin1200; -.
DR   EnsemblBacteria; CAC96431; CAC96431; CAC96431.
DR   KEGG; lin:racE; -.
DR   eggNOG; ENOG4105F03; Bacteria.
DR   eggNOG; COG0796; LUCA.
DR   HOGENOM; HOG000262396; -.
DR   KO; K01776; -.
DR   OMA; VYGCTHY; -.
DR   OrthoDB; 1718671at2; -.
DR   BioCyc; GCF_000195795:LIN_RS06120-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002513; 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; 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;
DR   PRODOM; Q92CH2.
DR   SWISS-2DPAGE; Q92CH2.
KW   Cell shape; Cell wall biogenesis/degradation; Isomerase;
KW   Peptidoglycan synthesis.
FT   CHAIN           1..266
FT                   /note="Glutamate racemase"
FT                   /id="PRO_0000095485"
FT   REGION          9..10
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   REGION          41..42
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   REGION          73..74
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   REGION          184..185
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   ACT_SITE        72
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
FT   ACT_SITE        183
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00258"
SQ   SEQUENCE   266 AA;  29146 MW;  CA9549098AB873AB CRC64;
     MKQAIGFIDS GVGGLTVVRE VLKQLPHEQV YYLGDTARCP YGPRDKEEVA QFTWEMTNFL
     VDRGIKMLVI ACNTATAAAL YDIREKLDIP VIGVIQPGSR AALKATRNNK IGVLGTLGTV
     ESMAYPTALK GLNRRVEVDS LACPKFVSVV ESGEYKSAIA KKVVAESLLP LKSTKIDTVI
     LGCTHYPLLK PIIENFMGDG VAVINSGEET ASEVSALLDY HNLLDATDDE IEHRFFTTGS
     TQIFKDIAKD WLNMPDMTVE HIKLGK
//

If you have problems or comments...

PBIL Back to PBIL home page