TRPF_KLULA
ID TRPF_KLULA Reviewed; 210 AA.
AC P13997;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase;
DE Short=PRAI;
DE EC=5.3.1.24;
GN Name=TRP1; OrderedLocusNames=KLLA0E17699g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2538971; DOI=10.1002/yea.320050106;
RA Stark M.J.R., Milner J.S.;
RT "Cloning and analysis of the Kluyveromyces lactis TRP1 gene: a chromosomal
RT locus flanked by genes encoding inorganic pyrophosphatase and histone H3.";
RL Yeast 5:35-50(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; X14230; CAA32445.1; -; Genomic_DNA.
DR EMBL; CR382125; CAG99832.1; -; Genomic_DNA.
DR PIR; S07893; ISVKNL.
DR RefSeq; XP_454745.1; XM_454745.1.
DR AlphaFoldDB; P13997; -.
DR SMR; P13997; -.
DR STRING; 28985.XP_454745.1; -.
DR EnsemblFungi; CAG99832; CAG99832; KLLA0_E17645g.
DR GeneID; 2894278; -.
DR KEGG; kla:KLLA0_E17645g; -.
DR eggNOG; KOG4202; Eukaryota.
DR HOGENOM; CLU_076364_1_0_1; -.
DR InParanoid; P13997; -.
DR OMA; FYAKSPR; -.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000000598; Chromosome E.
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..210
FT /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT /id="PRO_0000154333"
SQ SEQUENCE 210 AA; 22880 MW; 0F406A05E83CFA95 CRC64;
MLVKVCGLQT VEAAKTAVDD GADYLGIICV PGRKRTIDSS VAKGISTAVH QQENVKGTKL
VGVFRNQSVD DVLQLYHEYN LDVIQLHGDE DIKEYRSLIP SSIPIIKRFQ FPQDCELLLD
LYEHVDNVLT LFDSGEGGTG EKLNWSAISS WSASHPEIKF IIAGGLNPDN VSVAINMLPN
AIGVDVSGGV ETDGIKDLEK VKLFIQQASQ