TRPF_SACK1
ID TRPF_SACK1 Reviewed; 226 AA.
AC Q5XQP9; J5RY70;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase;
DE Short=PRAI;
DE EC=5.3.1.24;
GN Name=TRP1;
OS Saccharomyces kudriavzevii (strain ATCC MYA-4449 / AS 2.2408 / CBS 8840 /
OS NBRC 1802 / NCYC 2889) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=226230;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889;
RX PubMed=15381776; DOI=10.1073/pnas.0404319101;
RA Hittinger C.T., Rokas A., Carroll S.B.;
RT "Parallel inactivation of multiple GAL pathway genes and ecological
RT diversification in yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14144-14149(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889;
RX PubMed=12775844; DOI=10.1126/science.1084337;
RA Cliften P.F., Sudarsanam P., Desikan A., Fulton L., Fulton B., Majors J.,
RA Waterston R., Cohen B.A., Johnston M.;
RT "Finding functional features in Saccharomyces genomes by phylogenetic
RT footprinting.";
RL Science 301:71-76(2003).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889;
RX PubMed=22384314; DOI=10.1534/g3.111.000273;
RA Scannell D.R., Zill O.A., Rokas A., Payen C., Dunham M.J., Eisen M.B.,
RA Rine J., Johnston M., Hittinger C.T.;
RT "The awesome power of yeast evolutionary genetics: New genome sequences and
RT strain resources for the Saccharomyces sensu stricto genus.";
RL G3 (Bethesda) 1:11-25(2011).
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; AY740027; AAU43745.1; -; Genomic_DNA.
DR EMBL; AACI03000993; EJT43161.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5XQP9; -.
DR SMR; Q5XQP9; -.
DR STRING; 226230.Q5XQP9; -.
DR EnsemblFungi; EJT43161; EJT43161; SKUD_110006.
DR HOGENOM; CLU_076364_1_0_1; -.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000002753; Unassembled WGS sequence.
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 Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..226
FT /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT /id="PRO_0000154336"
SQ SEQUENCE 226 AA; 24791 MW; 79E79FF6030BF5AC CRC64;
MSFVNIRSSR GPVVKVCGLQ SLKAAQCALD SDADLLGIIC VPGRERTVDP VVAMEISALV
RACRTSMSTP KYLVGVFRNQ SKEDVLRIAN DYGIDIVQLH GDEPWQEYQK FLGLPVIKRL
VFPRDCDILL STPSEKTHLF MPLFDSEAGG TGELLDWNSI SDWFAEQGNP ECLQFMLAGG
LTPENVSDAL QLHGVIGVDV SGGVETNGMK DMDKITNFVR NAKKES
