ID TRPD_BUCAP Reviewed; 335 AA. AC P42392; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 136. 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}; GN OrderedLocusNames=BUsg_269; OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Buchnera. OX NCBI_TaxID=198804; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8407819; DOI=10.1128/jb.175.20.6426-6432.1993; RA Munson M.A., Baumann P.; RT "Molecular cloning and nucleotide sequence of a putative trpDC(F)BA operon RT in Buchnera aphidicola (endosymbiont of the aphid Schizaphis graminum)."; RL J. Bacteriol. 175:6426-6432(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sg; RX PubMed=12089438; DOI=10.1126/science.1071278; RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.; RT "50 million years of genomic stasis in endosymbiotic bacteria."; RL Science 296:2376-2379(2002). 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; Evidence={ECO:0000255|HAMAP- CC 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}. 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; Z19055; CAA79498.1; -; Genomic_DNA. DR EMBL; AE013218; AAM67827.1; -; Genomic_DNA. DR PIR; A49897; A49897. DR RefSeq; WP_011053794.1; NC_004061.1. DR AlphaFoldDB; P42392; -. DR SMR; P42392; -. DR STRING; 198804.BUsg_269; -. DR GeneID; 75258852; -. DR KEGG; bas:BUsg_269; -. DR eggNOG; COG0547; Bacteria. DR HOGENOM; CLU_034315_3_0_6; -. DR UniPathway; UPA00035; UER00041. DR Proteomes; UP000000416; 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; 3.40.1030.10; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 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 NCBIfam; TIGR01245; trpD; 1. DR PANTHER; PTHR43285; ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE; 1. DR PANTHER; PTHR43285:SF2; ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE; 1. DR Pfam; PF02885; Glycos_trans_3N; 1. DR Pfam; PF00591; Glycos_transf_3; 1. DR SUPFAM; SSF52418; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1. DR SUPFAM; SSF47648; Nucleoside phosphorylase/phosphoribosyltransferase N-terminal domain; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Glycosyltransferase; Magnesium; Metal-binding; Transferase; KW Tryptophan biosynthesis. FT CHAIN 1..335 FT /note="Anthranilate phosphoribosyltransferase" FT /id="PRO_0000154435" FT BINDING 79 FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate" FT /ligand_id="ChEBI:CHEBI:58017" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT BINDING 79 FT /ligand="anthranilate" FT /ligand_id="ChEBI:CHEBI:16567" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT BINDING 82..83 FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate" FT /ligand_id="ChEBI:CHEBI:58017" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT BINDING 87 FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate" FT /ligand_id="ChEBI:CHEBI:58017" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT BINDING 89..92 FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate" FT /ligand_id="ChEBI:CHEBI:58017" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT BINDING 91 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT BINDING 107..115 FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate" FT /ligand_id="ChEBI:CHEBI:58017" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT BINDING 110 FT /ligand="anthranilate" FT /ligand_id="ChEBI:CHEBI:16567" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT BINDING 119 FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate" FT /ligand_id="ChEBI:CHEBI:58017" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT BINDING 165 FT /ligand="anthranilate" FT /ligand_id="ChEBI:CHEBI:16567" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT BINDING 223 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT BINDING 224 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT BINDING 224 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" SQ SEQUENCE 335 AA; 38090 MW; E33F51F2126013AD CRC64; MQNIFNKIYE SKSLNQEESY QLFKSIALGK INEIQLSSIL TAMQMHGESE KEILGAIYAF SERMKFFPRP NYIFSDIVGT GGDSKNTINV STSSAFVAAS CGFKIIKHCN KGVSSKSGSS DLLNKFKINL NTSLENSKKI LDKLNICFLF APKYHSVFKY ASKTRSILKI KTIFNLLGPF LNPSRPPLTL IGVYKKDLVN PMSRILKKLK YQRGIILHGD DTDEVTLHGT TYISELLNNK IYSYELEPED FGIKRHSKSI FVEYSPEENY HIIKKTMQGK GEKLHEELIA VNVALLLKIF GHENLKENTK IALKKIRSGD VYKHIMQVSN MLKED //