(data stored in SCRATCH9089 zone)

SWISSPROT: TRPD_PASMU

ID   TRPD_PASMU              Reviewed;         333 AA.
AC   P57856;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   11-DEC-2019, entry version 120.
DE   RecName: Full=Anthranilate phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00211};
DE            EC=2.4.2.18 {ECO:0000255|HAMAP-Rule:MF_00211};
GN   Name=trpD {ECO:0000255|HAMAP-Rule:MF_00211}; OrderedLocusNames=PM0581;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- FUNCTION: Catalyzes the transfer of the phosphoribosyl group of 5-
CC       phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-
CC       phosphoribosyl)-anthranilate (PRA). {ECO:0000255|HAMAP-Rule:MF_00211}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-
CC         phospho-alpha-D-ribose 1-diphosphate + anthranilate;
CC         Xref=Rhea:RHEA:11768, ChEBI:CHEBI:16567, ChEBI:CHEBI:18277,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58017; EC=2.4.2.18;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00211};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00211};
CC       Note=Binds 2 magnesium ions per monomer. {ECO:0000255|HAMAP-
CC       Rule:MF_00211};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 2/5. {ECO:0000255|HAMAP-
CC       Rule:MF_00211}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00211}.
CC   -!- SIMILARITY: Belongs to the anthranilate phosphoribosyltransferase
CC       family. {ECO:0000255|HAMAP-Rule:MF_00211}.
DR   EMBL; AE004439; AAK02665.1; -; Genomic_DNA.
DR   RefSeq; WP_005722087.1; NC_002663.1.
DR   SMR; P57856; -.
DR   EnsemblBacteria; AAK02665; AAK02665; PM0581.
DR   GeneID; 29387760; -.
DR   KEGG; pmu:PM0581; -.
DR   eggNOG; ENOG4108I0Q; Bacteria.
DR   eggNOG; COG0547; LUCA.
DR   HOGENOM; HOG000230451; -.
DR   KO; K00766; -.
DR   OMA; HHSAMKH; -.
DR   BioCyc; PMUL272843:G1FZ8-613-MONOMER; -.
DR   UniPathway; UPA00035; UER00041.
DR   Proteomes; UP000000809; Chromosome.
DR   GO; GO:0004048; F:anthranilate phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.970.10; -; 1.
DR   Gene3D; 3.40.1030.10; -; 1.
DR   HAMAP; MF_00211; TrpD; 1.
DR   InterPro; IPR005940; Anthranilate_Pribosyl_Tfrase.
DR   InterPro; IPR000312; Glycosyl_Trfase_fam3.
DR   InterPro; IPR017459; Glycosyl_Trfase_fam3_N_dom.
DR   InterPro; IPR036320; Glycosyl_Trfase_fam3_N_dom)sf.
DR   InterPro; IPR035902; Nuc_phospho_transferase.
DR   Pfam; PF02885; Glycos_trans_3N; 1.
DR   Pfam; PF00591; Glycos_transf_3; 1.
DR   SUPFAM; SSF47648; SSF47648; 1.
DR   SUPFAM; SSF52418; SSF52418; 1.
DR   TIGRFAMs; TIGR01245; trpD; 1.
PE   3: Inferred from homology;
DR   PRODOM; P57856.
DR   SWISS-2DPAGE; P57856.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Glycosyltransferase; Magnesium; Metal-binding; Reference proteome;
KW   Transferase; Tryptophan biosynthesis.
FT   CHAIN           1..333
FT                   /note="Anthranilate phosphoribosyltransferase"
FT                   /id="PRO_0000154467"
FT   REGION          84..85
FT                   /note="Phosphoribosylpyrophosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   REGION          91..94
FT                   /note="Phosphoribosylpyrophosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   REGION          109..117
FT                   /note="Phosphoribosylpyrophosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   METAL           93
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   METAL           225
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   METAL           226
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   METAL           226
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         81
FT                   /note="Anthranilate 1; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         81
FT                   /note="Phosphoribosylpyrophosphate; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         89
FT                   /note="Phosphoribosylpyrophosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         112
FT                   /note="Anthranilate 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         121
FT                   /note="Phosphoribosylpyrophosphate; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
FT   BINDING         167
FT                   /note="Anthranilate 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00211"
SQ   SEQUENCE   333 AA;  35880 MW;  F42760CD105F6C5A CRC64;
     MQTEQLLHQL FEKKALNQQQ TEFLFTAIVR GQLDNSQLSA ALIALKLRGE TPEEISGAVT
     ALQADAESFP IPDYPFADIV GTGGDGANTI NISTASAIVA ASYGLKVAKH GNRSVSSQTG
     ASDLLTALGV NVHISAHKAR QALDEIGLCF LFAPQYHLGF QHAIPVRQAL KTRTIFNILG
     PLINPAKPKR QLLGVYSSDL IQPYAETVAR LGHEHSVVVH GSGLDEIALH GVTEVAEIKA
     GQIERYTLTP QDFGFQPQPL ETLRGGKPSE NAQILTALLQ GKGKLAHQQA VAMNSAMLMS
     LFGYPNLKQN AQAIMDIIAT GKPFETLQQL TQY
//

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