TRPF_ZYGBA
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 25-MAY-2022, entry version 62.
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}.
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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; -; 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; PTHR42894; 1.
DR Pfam; PF00697; PRAI; 1.
DR SUPFAM; SSF51366; SSF51366; 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