ID TRPF_SYNY3 Reviewed; 218 AA. AC P74435; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 27-MAR-2024, entry version 121. DE RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase; DE Short=PRAI; DE EC=5.3.1.24; GN Name=trpF; OrderedLocusNames=sll0356; OS Synechocystis sp. (strain PCC 6803 / Kazusa). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae; OC Synechocystis. OX NCBI_TaxID=1111708; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 6803 / Kazusa; RX PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire RT genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). 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; CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 3/5. CC -!- SIMILARITY: Belongs to the TrpF family. {ECO:0000305}. 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; BA000022; BAA18536.1; -; Genomic_DNA. DR PIR; S76407; S76407. DR AlphaFoldDB; P74435; -. DR SMR; P74435; -. DR STRING; 1148.gene:10499418; -. DR PaxDb; 1148-1653624; -. DR EnsemblBacteria; BAA18536; BAA18536; BAA18536. DR KEGG; syn:sll0356; -. DR eggNOG; COG0135; Bacteria. DR InParanoid; P74435; -. DR PhylomeDB; P74435; -. DR UniPathway; UPA00035; UER00042. DR Proteomes; UP000001425; Chromosome. DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IBA:GO_Central. DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central. 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 Reference proteome; Tryptophan biosynthesis. FT CHAIN 1..218 FT /note="N-(5'-phosphoribosyl)anthranilate isomerase" FT /id="PRO_0000154389" SQ SEQUENCE 218 AA; 23881 MW; 37D6035030C55A4F CRC64; MAMEVKICGL RHPAQAQAIA ALGFTTLGFI CVEASSRYVS SREIELVLQS LTAHNKRSAI GVFANVSLPK LGEFLAQTSL NGIQLHGDES PDFCRQVKQA FPQHRLIKAL RLRRSADLER AEAYYNAVDV LLLDAYHPEQ LGGTGQTLPW QKLQQFRPPL PWWLAGGLTP SNVQEALNLL QPDGIDLSSG VEQGPADKDV AKVAQLRAQL DALAILQH //