ID TRPF_ZYGBA Reviewed; 205 AA. AC Q9HFW8; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 22-FEB-2023, entry version 64. DE RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase; DE Short=PRAI; DE EC=5.3.1.24; GN Name=TRP1; OS Zygosaccharomyces bailii. OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces. OX NCBI_TaxID=4954; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=CBS 685 / NCYC 563 / NRRL Y-12949; RX PubMed=11169759; RX DOI=10.1002/1097-0061(20010130)18:2<173::aid-yea663>3.0.co;2-f; RA Mollapour M., Piper P.W.; RT "Targeted gene deletion in Zygosaccharomyces bailii."; RL Yeast 18:173-186(2001). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ISA 1307; RA Rodrigues F.J., Steensma Y., Corte-Real M.S.; RT "Sequence analyses of a Zygosaccharomyces bailii DNA fragment containing RT the Thr-tRNA, IPP1 and TRP1 genes."; RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases. 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; AF279262; AAG17697.1; -; Genomic_DNA. DR EMBL; AJ309279; CAC37331.1; -; Genomic_DNA. DR AlphaFoldDB; Q9HFW8; -. DR SMR; Q9HFW8; -. DR UniPathway; UPA00035; UER00042. DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:UniProtKB-EC. DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway. 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..205 FT /note="N-(5'-phosphoribosyl)anthranilate isomerase" FT /id="PRO_0000154338" SQ SEQUENCE 205 AA; 22316 MW; DECD9AE9F0DDBC0E CRC64; MIAKICGLQS VEAAQQAVDN GADLIGVICV PNRKRTVDPE IARSISKICH GTGTRLVGVF RNQPKEEVRQ LAQEYELDVV QLHGDEDWQE YASYVGLPLL KRVVFPRDVS LVSQMDGEVC TPLFDSEAGG SGEKLDWQAI GSWFQDSQLT RGYLLAGGLS PDNVVEALRV PGVVGVDVSG GVETDGTKDL AKIKQFLELY KVNVN //