ID TRPD_PSEAE Reviewed; 349 AA. AC P20574; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 02-SEP-2026, entry version 151. 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=PA0650; OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pseudomonadales; Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208964; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2105306; DOI=10.1128/jb.172.2.853-866.1990; RA Essar D.W., Eberly L., Han C.Y., Crawford I.P.; RT "DNA sequences and characterization of four early genes of the tryptophan RT pathway in Pseudomonas aeruginosa."; RL J. Bacteriol. 172:853-866(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1; RX PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic RT pathogen."; RL Nature 406:959-964(2000). 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=N-(5-phospho-beta-D-ribosyl)anthranilate + diphosphate = 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; M33814; AAA25824.1; -; Genomic_DNA. DR EMBL; AE004091; AAG04039.1; -; Genomic_DNA. DR PIR; B35114; B35114. DR RefSeq; NP_249341.1; NC_002516.2. DR RefSeq; WP_003085203.1; NC_002516.2. DR AlphaFoldDB; P20574; -. DR SMR; P20574; -. DR FunCoup; P20574; 507. DR STRING; 208964.PA0650; -. DR PaxDb; 208964-PA0650; -. DR GeneID; 880665; -. DR KEGG; pae:PA0650; -. DR PATRIC; fig|208964.12.peg.681; -. DR PseudoCAP; PA0650; -. DR HOGENOM; CLU_034315_2_1_6; -. DR InParanoid; P20574; -. DR OrthoDB; 9806430at2; -. DR PhylomeDB; P20574; -. DR BioCyc; PAER208964:G1FZ6-655-MONOMER; -. DR UniPathway; UPA00035; UER00041. DR Proteomes; UP000002438; Chromosome. DR AbasyAtlas; P20574; -. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. 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:L-tryptophan biosynthetic process; IEA:UniProtKB-UniRule. DR FunFam; 1.20.970.10:FF:000006; Anthranilate phosphoribosyltransferase; 1. DR FunFam; 3.40.1030.10:FF:000002; Anthranilate phosphoribosyltransferase; 1. DR Gene3D; 3.40.1030.10; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1. DR Gene3D; 1.20.970.10; Transferase, Pyrimidine Nucleoside Phosphorylase, Chain C; 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..349 FT /note="Anthranilate phosphoribosyltransferase" FT /id="PRO_0000154468" FT BINDING 82 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 82 FT /ligand="anthranilate" FT /ligand_id="ChEBI:CHEBI:16567" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT BINDING 85..86 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 92..95 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 94 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT BINDING 110..118 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 113 FT /ligand="anthranilate" FT /ligand_id="ChEBI:CHEBI:16567" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT BINDING 122 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 168 FT /ligand="anthranilate" FT /ligand_id="ChEBI:CHEBI:16567" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT BINDING 227 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT BINDING 228 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" FT BINDING 228 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00211" SQ SEQUENCE 349 AA; 37384 MW; CAC05F684969BA4B CRC64; MDIKGALNRI VNQLDLTTEE MQAVMRQIMT GQCTDAQIGA FLMGMRMKSE TIDEIVGAVA VMRELADGVQ LPTLKHVVDV VGTGGDGANI FNVSSAASFV VAAAGGKVAK HGNRAVSGKS GSADLLEAAG IYLELTSEQV ARCIDTVGVG FMFAQVHHKA MKYAAGPRRE LGLRTLFNML GPLTNPAGVR HQVVGVFTQE LCKPLAEVLK RLGSEHVLVV HSRDGLDEFS LAAATHIAEL KDGEVREYEV RPEDFGIKSQ TLMGLEVDSP QASLELIRDA LGRRKTEAGQ KAAELIVMNA GPALYAADLA TSLHEGIQLA HDALHTGLAR EKMDELVAFT AVYREENAQ //