ID TRPD_BRUA2 Reviewed; 339 AA. AC Q2YRR5; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 07-FEB-2006, sequence version 1. DT 27-MAR-2024, entry version 89. 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=BAB1_1163; OS Brucella abortus (strain 2308). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Brucellaceae; Brucella/Ochrobactrum group; Brucella. OX NCBI_TaxID=359391; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2308; RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005; RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.; RT "Whole-genome analyses of speciation events in pathogenic Brucellae."; RL Infect. Immun. 73:8353-8361(2005). 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; AM040264; CAJ11119.1; -; Genomic_DNA. DR RefSeq; WP_002969119.1; NZ_KN046823.1. DR AlphaFoldDB; Q2YRR5; -. DR SMR; Q2YRR5; -. DR STRING; 359391.BAB1_1163; -. DR GeneID; 3787802; -. DR KEGG; bmf:BAB1_1163; -. DR PATRIC; fig|359391.11.peg.61; -. DR HOGENOM; CLU_034315_2_1_5; -. DR UniPathway; UPA00035; UER00041. DR Proteomes; UP000002719; Chromosome I. 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; Reference proteome; KW Transferase; Tryptophan biosynthesis. FT CHAIN 1..339 FT /note="Anthranilate phosphoribosyltransferase" FT /id="PRO_0000227140" FT BINDING 81 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 81 FT /ligand="anthranilate" FT /ligand_id="ChEBI:CHEBI:16567" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT BINDING 84..85 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 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..94 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 93 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT BINDING 109..117 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 112 FT /ligand="anthranilate" FT /ligand_id="ChEBI:CHEBI:16567" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT BINDING 121 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 167 FT /ligand="anthranilate" FT /ligand_id="ChEBI:CHEBI:16567" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT BINDING 225 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT BINDING 226 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT BINDING 226 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" SQ SEQUENCE 339 AA; 34839 MW; 182891532AE4FCDA CRC64; MADLKPYIAK AASGEPLPLG DAKAAFDIMM SGQATPSQIG GFLMALRVRG ETVPEIAGAV ASMRSRMIPV IAPDDAMDIV GTGGDQSGSY NVSSCTAFVV AGAGVPVAKH GNRALSSRSG AADALAALGI NIEADADTIG RSISEAGLGF MFAPMHHSAM RHVGPSRVEL GTRTIFNLLG PLSNPASVKR QLVGVFAPQW LEPLAHVLKE LGSETAWVVY GDGLDEMTTA GTTQVAALEN GQIRTFEITP EEVGLRRCSP AELKGGEAAE NAKALLGVLE GKDSAYRDIV LLNSGAALVV AGKAENLKDG IAQAVQSIDS GAALAVLQKV IAVSNDKPA //