ID   TRPF_LIPST              Reviewed;         232 AA.
AC   Q01128;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   22-FEB-2023, entry version 78.
DE   RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase;
DE            Short=PRAI;
DE            EC=5.3.1.24;
GN   Name=TRP1;
OS   Lipomyces starkeyi (Oleaginous yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Lipomycetaceae; Lipomyces.
OX   NCBI_TaxID=29829;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 12659 / NCYC 1436 / NRRL Y-1389;
RX   PubMed=8662214; DOI=10.1007/s002940050104;
RA   Bignell G.R., Bruce I.J., Evans I.H.;
RT   "Electrophoretic karyotype of the amylolytic yeast Lipomyces starkeyi and
RT   cloning, sequencing and chromosomal localization of its TRP1 gene.";
RL   Curr. Genet. 30:83-88(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}.
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DR   EMBL; Z68292; CAA92584.1; -; Genomic_DNA.
DR   PIR; S70355; S70355.
DR   AlphaFoldDB; Q01128; -.
DR   SMR; Q01128; -.
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_0000154334"
SQ   SEQUENCE   232 AA;  24625 MW;  E6FF1B4EA7D7A9E0 CRC64;
     MTVSTTSLCT PIVKICGLTV EAAHCAISSG ADLIGMILVP DLKRTVQQTK LKAISRAVTR
     IPGVPTSPSR GIDRPSHGLV RGTFSADYTS WPLVVGVFRN QSLDEVLRML RNYDLDIVQL
     HGSEPLHQWT REIPVPVIKK FGLGEDDLMA PGLHAVTLLD GGAGGEGQKI SWEGLPGSGA
     FMLAGGLTVD NVAVAVKIPN VAGVDVSSGV ATDGMQDLEK NCRCLFRNAK GW
//