ID TRPF_XYLF2 Reviewed; 220 AA. AC B2I9J1; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-JUN-2008, sequence version 1. DT 27-MAR-2024, entry version 68. DE RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase {ECO:0000255|HAMAP-Rule:MF_00135}; DE Short=PRAI {ECO:0000255|HAMAP-Rule:MF_00135}; DE EC=5.3.1.24 {ECO:0000255|HAMAP-Rule:MF_00135}; GN Name=trpF {ECO:0000255|HAMAP-Rule:MF_00135}; GN OrderedLocusNames=XfasM23_0643; OS Xylella fastidiosa (strain M23). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=405441; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M23; RX PubMed=20601474; DOI=10.1128/jb.00651-10; RA Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.; RT "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23) RT causing almond leaf scorch disease in California."; RL J. Bacteriol. 192:4534-4534(2010). CC -!- CATALYTIC ACTIVITY: CC Reaction=N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2- CC carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate; CC Xref=Rhea:RHEA:21540, ChEBI:CHEBI:18277, ChEBI:CHEBI:58613; CC EC=5.3.1.24; Evidence={ECO:0000255|HAMAP-Rule:MF_00135}; CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 3/5. {ECO:0000255|HAMAP- CC Rule:MF_00135}. CC -!- SIMILARITY: Belongs to the TrpF family. {ECO:0000255|HAMAP- CC Rule:MF_00135}. 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; CP001011; ACB92085.1; -; Genomic_DNA. DR RefSeq; WP_004090663.1; NC_010577.1. DR AlphaFoldDB; B2I9J1; -. DR SMR; B2I9J1; -. DR GeneID; 58016158; -. DR KEGG; xfn:XfasM23_0643; -. DR HOGENOM; CLU_076364_2_0_6; -. DR UniPathway; UPA00035; UER00042. DR Proteomes; UP000001698; Chromosome. DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd00405; PRAI; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR HAMAP; MF_00135; PRAI; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001240; PRAI_dom. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR InterPro; IPR044643; TrpF_fam. DR PANTHER; PTHR42894; N-(5'-PHOSPHORIBOSYL)ANTHRANILATE ISOMERASE; 1. DR PANTHER; PTHR42894:SF1; N-(5'-PHOSPHORIBOSYL)ANTHRANILATE ISOMERASE; 1. DR Pfam; PF00697; PRAI; 1. DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Isomerase; KW Tryptophan biosynthesis. FT CHAIN 1..220 FT /note="N-(5'-phosphoribosyl)anthranilate isomerase" FT /id="PRO_1000095952" SQ SEQUENCE 220 AA; 24113 MW; CDA01684E375DC31 CRC64; MNIPPYRTRI KFCGMTRVGD VRLASELGVD AVGLIFASGS SRLLTVSAAC AIRRTVAPMV DVVALFQNNS ADEIHTVVRT VRPTLLQFHG KEEDAFCRTF NVPYLKAIPM AGAEAKRICT RTLYLKYPNA AGFIFDSHLK GGTGQTFDWS RLPIDLHHPF LLAGGITPEN VFDAIAATVP WGVDVSSGIE LQPGIKDGDK MRQFVEEVRR ADGRRLLGVP //