ID   TRPF_WICAO              Reviewed;         232 AA.
AC   Q875I3;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   22-FEB-2023, entry version 67.
DE   RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase;
DE            Short=PRAI;
DE            EC=5.3.1.24;
GN   Name=TRP1;
OS   Wickerhamomyces anomalus (Yeast) (Hansenula anomala).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX   NCBI_TaxID=4927;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K;
RX   PubMed=14663825; DOI=10.1002/yea.1033;
RA   Friel D., Vandenbol M., Jijakli M.H.;
RT   "Cloning and sequence analysis of the TRP1 gene encoding the phosphoribosyl
RT   anthranilate isomerase from Pichia anomala (strain K).";
RL   Yeast 20:1331-1337(2003).
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}.
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DR   EMBL; AY198188; AAO19636.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q875I3; -.
DR   SMR; Q875I3; -.
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..232
FT                   /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT                   /id="PRO_0000154332"
SQ   SEQUENCE   232 AA;  25553 MW;  122926A9FC253680 CRC64;
     MLVKICGVKD VEAAQVALES GADMIGMIFV PGKPRTIQVS NAKEVVSLVE SKRKGLNSNE
     LYDSLKPGQD SLWFEQVHDS IKSNGPYSVG VFRNQSIEEI NNIIEEVDID FVQLHGQESH
     DEYIPQLKKP VITRFVPNET KVLQSLKPNK HLLPLFDSEA GGEGVKLNWS NLSDWSAKNN
     ARYLLAGGLT PDNVHEAIKL DGVIGVDVSG GVETNGVKDY VKIKEFVKNA LQ
//