TRPF_YEAST
ID TRPF_YEAST Reviewed; 224 AA.
AC P00912; D6VRZ5; Q03448; Q12131; Q70DA4; Q70DA7; Q70DB2; Q7LHE0;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase;
DE Short=PRAI;
DE EC=5.3.1.24;
GN Name=TRP1; OrderedLocusNames=YDR007W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6248420; DOI=10.1016/0378-1119(80)90133-x;
RA Tschumper G., Carbon J.;
RT "Sequence of a yeast DNA fragment containing a chromosomal replicator and
RT the TRP1 gene.";
RL Gene 10:157-166(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8154181; DOI=10.1002/yea.320091203;
RA Brunelli J.P., Pall M.L.;
RT "A series of yeast shuttle vectors for expression of cDNAs and other DNA
RT sequences.";
RL Yeast 9:1299-1308(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lieberman B.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-48; ARG-172 AND
RP PHE-212.
RC STRAIN=ATCC 204508 / S288c, CLIB 219, CLIB 382, CLIB 388, CLIB 410,
RC CLIB 413, CLIB 556, CLIB 630, CLIB 95, K1, R12, R13, Sigma 1278B, YIIc12,
RC and YIIc17;
RX PubMed=15087486; DOI=10.1093/nar/gkh529;
RA Leh-Louis V., Wirth B., Despons L., Wain-Hobson S., Potier S.,
RA Souciet J.-L.;
RT "Differential evolution of the Saccharomyces cerevisiae DUP240 paralogs and
RT implication of recombination in phylogeny.";
RL Nucleic Acids Res. 32:2069-2078(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 206-224.
RX PubMed=3785376; DOI=10.1038/324087a0;
RA Snyder M., Buchman A.R., Davis R.W.;
RT "Bent DNA at a yeast autonomously replicating sequence.";
RL Nature 324:87-89(1986).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(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 -!- MISCELLANEOUS: Present with 1850 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TrpF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA80674.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA88067.1; Type=Erroneous termination; Note=Truncated C-terminus. This mutation is only found in the substrain S288c / AB972. The S288c reference strain does not contain this mutation.; Evidence={ECO:0000305};
CC Sequence=CAA88068.1; Type=Erroneous termination; Note=Truncated C-terminus. This mutation is only found in the substrain S288c / AB972. The S288c reference strain does not contain this mutation.; Evidence={ECO:0000305};
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DR EMBL; V01341; CAA24634.1; -; Genomic_DNA.
DR EMBL; M74015; AAA72097.1; -; Genomic_DNA.
DR EMBL; U37458; AAA80674.1; ALT_INIT; Genomic_DNA.
DR EMBL; AJ585667; CAE52187.1; -; Genomic_DNA.
DR EMBL; AJ585668; CAE52188.1; -; Genomic_DNA.
DR EMBL; AJ585669; CAE52189.1; -; Genomic_DNA.
DR EMBL; AJ585670; CAE52190.1; -; Genomic_DNA.
DR EMBL; AJ585671; CAE52191.1; -; Genomic_DNA.
DR EMBL; AJ585672; CAE52192.1; -; Genomic_DNA.
DR EMBL; AJ585673; CAE52193.1; -; Genomic_DNA.
DR EMBL; AJ585674; CAE52194.1; -; Genomic_DNA.
DR EMBL; AJ585675; CAE52195.1; -; Genomic_DNA.
DR EMBL; AJ585676; CAE52196.1; -; Genomic_DNA.
DR EMBL; AJ585677; CAE52197.1; -; Genomic_DNA.
DR EMBL; AJ585678; CAE52198.1; -; Genomic_DNA.
DR EMBL; AJ585679; CAE52199.1; -; Genomic_DNA.
DR EMBL; AJ585680; CAE52200.1; -; Genomic_DNA.
DR EMBL; AJ585681; CAE52201.1; -; Genomic_DNA.
DR EMBL; AJ585682; CAE52202.1; -; Genomic_DNA.
DR EMBL; AJ585683; CAE52203.1; -; Genomic_DNA.
DR EMBL; AJ585684; CAE52204.1; -; Genomic_DNA.
DR EMBL; AJ585685; CAE52205.1; -; Genomic_DNA.
DR EMBL; Z48008; CAA88067.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z48008; CAA88068.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M30386; AAA18406.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11855.1; -; Genomic_DNA.
DR PIR; A01135; ISBYN.
DR RefSeq; NP_010290.3; NM_001180315.3.
DR AlphaFoldDB; P00912; -.
DR SMR; P00912; -.
DR BioGRID; 32060; 112.
DR DIP; DIP-2671N; -.
DR IntAct; P00912; 1.
DR MINT; P00912; -.
DR STRING; 4932.YDR007W; -.
DR iPTMnet; P00912; -.
DR MaxQB; P00912; -.
DR PaxDb; P00912; -.
DR PRIDE; P00912; -.
DR EnsemblFungi; YDR007W_mRNA; YDR007W; YDR007W.
DR GeneID; 851570; -.
DR KEGG; sce:YDR007W; -.
DR SGD; S000002414; TRP1.
DR VEuPathDB; FungiDB:YDR007W; -.
DR eggNOG; KOG4202; Eukaryota.
DR HOGENOM; CLU_076364_1_0_1; -.
DR OMA; FYAKSPR; -.
DR BioCyc; YEAST:YDR007W-MON; -.
DR UniPathway; UPA00035; UER00042.
DR PRO; PR:P00912; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P00912; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IDA:SGD.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IDA:SGD.
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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Isomerase;
KW Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..224
FT /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT /id="PRO_0000154337"
FT VARIANT 48
FT /note="I -> V (in strain: CLIB 556 haplotype Ha2 and CLIB
FT 630 haplotype Ha2)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 172
FT /note="S -> R (in strain: CLIB 556 haplotype Ha1)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 212
FT /note="S -> F (in strain: CLIB 95, CLIB 382, CLIB 388, CLIB
FT 556 haplotype Ha2, CLIB 630, K1, R12, R13, YIIc12 haplotype
FT Ha2 and YIIc17 haplotype Ha1)"
FT /evidence="ECO:0000269|PubMed:15087486"
SQ SEQUENCE 224 AA; 24144 MW; 03353B85F24FA09D CRC64;
MSVINFTGSS GPLVKVCGLQ STEAAECALD SDADLLGIIC VPNRKRTIDP VIARKISSLV
KAYKNSSGTP KYLVGVFRNQ PKEDVLALVN DYGIDIVQLH GDESWQEYQE FLGLPVIKRL
VFPKDCNILL SAASQKPHSF IPLFDSEAGG TGELLDWNSI SDWVGRQESP ESLHFMLAGG
LTPENVGDAL RLNGVIGVDV SGGVETNGVK DSNKIANFVK NAKK
