TRPD_YEAST
ID TRPD_YEAST Reviewed; 380 AA.
AC P07285; D6VSY4;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Anthranilate phosphoribosyltransferase {ECO:0000303|PubMed:2428012};
DE Short=PRtransferase;
DE EC=2.4.2.18 {ECO:0000269|PubMed:2428012};
GN Name=TRP4 {ECO:0000303|PubMed:2428012}; OrderedLocusNames=YDR354W;
GN ORFNames=D9476.4;
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], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=2428012; DOI=10.1093/nar/14.16.6357;
RA Furter R., Paravicini G., Aebi M., Braus G., Prantl F., Niederberger P.,
RA Huetter R.;
RT "The TRP4 gene of Saccharomyces cerevisiae: isolation and structural
RT analysis.";
RL Nucleic Acids Res. 14:6357-6373(1986).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 202-380.
RX PubMed=7503995; DOI=10.1083/jcb.123.5.1175;
RA Kilmartin J.V., Dyos S.L., Kershaw D., Finch J.T.;
RT "A spacer protein in the Saccharomyces cerevisiae spindle poly body whose
RT transcript is cell cycle-regulated.";
RL J. Cell Biol. 123:1175-1184(1993).
RN [5]
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 -!- FUNCTION: Catalyzes the transfer of the phosphoribosyl group of 5-
CC phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-
CC phosphoribosyl)-anthranilate (PRA), the second step in tryptophan
CC biosynthesis. {ECO:0000305|PubMed:2428012}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-
CC phospho-alpha-D-ribose 1-diphosphate + anthranilate;
CC Xref=Rhea:RHEA:11768, ChEBI:CHEBI:16567, ChEBI:CHEBI:18277,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58017; EC=2.4.2.18;
CC Evidence={ECO:0000269|PubMed:2428012};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11770;
CC Evidence={ECO:0000305|PubMed:2428012};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 2/5. {ECO:0000305|PubMed:2428012}.
CC -!- MISCELLANEOUS: Present with 1760 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the anthranilate phosphoribosyltransferase
CC family. {ECO:0000305}.
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DR EMBL; X04273; CAA27822.1; -; Genomic_DNA.
DR EMBL; U28372; AAB64790.1; -; Genomic_DNA.
DR EMBL; X73297; CAA51732.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12194.1; -; Genomic_DNA.
DR PIR; S05865; NPBY.
DR RefSeq; NP_010641.3; NM_001180662.3.
DR PDB; 7DSJ; X-ray; 2.44 A; A/B=1-380.
DR PDB; 7DSM; X-ray; 2.39 A; A/B=1-380.
DR PDB; 7DSO; X-ray; 2.34 A; A/B=1-380.
DR PDB; 7DSP; X-ray; 1.95 A; A/B=1-380.
DR PDB; 7DSR; X-ray; 2.50 A; A/B=1-380.
DR PDBsum; 7DSJ; -.
DR PDBsum; 7DSM; -.
DR PDBsum; 7DSO; -.
DR PDBsum; 7DSP; -.
DR PDBsum; 7DSR; -.
DR AlphaFoldDB; P07285; -.
DR SMR; P07285; -.
DR BioGRID; 32411; 171.
DR IntAct; P07285; 2.
DR MINT; P07285; -.
DR STRING; 4932.YDR354W; -.
DR MaxQB; P07285; -.
DR PaxDb; P07285; -.
DR PRIDE; P07285; -.
DR EnsemblFungi; YDR354W_mRNA; YDR354W; YDR354W.
DR GeneID; 851956; -.
DR KEGG; sce:YDR354W; -.
DR SGD; S000002762; TRP4.
DR VEuPathDB; FungiDB:YDR354W; -.
DR eggNOG; KOG1438; Eukaryota.
DR HOGENOM; CLU_034315_2_1_1; -.
DR InParanoid; P07285; -.
DR OMA; GPMTNPA; -.
DR BioCyc; YEAST:YDR354W-MON; -.
DR UniPathway; UPA00035; UER00041.
DR PRO; PR:P07285; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P07285; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0004048; F:anthranilate phosphoribosyltransferase activity; IDA:SGD.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IMP:SGD.
DR Gene3D; 3.40.1030.10; -; 1.
DR InterPro; IPR005940; Anthranilate_Pribosyl_Tfrase.
DR InterPro; IPR000312; Glycosyl_Trfase_fam3.
DR InterPro; IPR017459; Glycosyl_Trfase_fam3_N_dom.
DR InterPro; IPR035902; Nuc_phospho_transferase.
DR PANTHER; PTHR43285; PTHR43285; 1.
DR Pfam; PF02885; Glycos_trans_3N; 1.
DR Pfam; PF00591; Glycos_transf_3; 1.
DR SUPFAM; SSF52418; SSF52418; 1.
DR TIGRFAMs; TIGR01245; trpD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Glycosyltransferase; Reference proteome; Transferase;
KW Tryptophan biosynthesis.
FT CHAIN 1..380
FT /note="Anthranilate phosphoribosyltransferase"
FT /id="PRO_0000154528"
FT HELIX 3..14
FT /evidence="ECO:0007829|PDB:7DSP"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:7DSP"
FT HELIX 22..37
FT /evidence="ECO:0007829|PDB:7DSP"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:7DSJ"
FT HELIX 44..63
FT /evidence="ECO:0007829|PDB:7DSP"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:7DSP"
FT HELIX 69..80
FT /evidence="ECO:0007829|PDB:7DSP"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:7DSP"
FT HELIX 120..129
FT /evidence="ECO:0007829|PDB:7DSP"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:7DSP"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:7DSJ"
FT HELIX 153..157
FT /evidence="ECO:0007829|PDB:7DSP"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:7DSP"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:7DSP"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:7DSP"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:7DSP"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:7DSP"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:7DSP"
FT HELIX 188..200
FT /evidence="ECO:0007829|PDB:7DSP"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:7DSP"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:7DSP"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:7DSP"
FT HELIX 231..242
FT /evidence="ECO:0007829|PDB:7DSP"
FT STRAND 247..253
FT /evidence="ECO:0007829|PDB:7DSP"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:7DSP"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:7DSP"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:7DSP"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:7DSP"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:7DSP"
FT HELIX 287..290
FT /evidence="ECO:0007829|PDB:7DSP"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:7DSP"
FT HELIX 305..314
FT /evidence="ECO:0007829|PDB:7DSP"
FT TURN 315..318
FT /evidence="ECO:0007829|PDB:7DSP"
FT HELIX 328..345
FT /evidence="ECO:0007829|PDB:7DSP"
FT HELIX 350..362
FT /evidence="ECO:0007829|PDB:7DSP"
FT HELIX 365..378
FT /evidence="ECO:0007829|PDB:7DSP"
SQ SEQUENCE 380 AA; 41374 MW; 9E231587F085F32B CRC64;
MSEATLLSYT KKLLASPPQL SSTDLHDALL VILSLLQKCD TNSDESLSIY TKVSSFLTAL
RVTKLDHKAE YIAEAAKAVL RHSDLVDLPL PKKDELHPED GPVILDIVGT GGDGQNTFNV
STSAAIVASG IQGLKICKHG GKASTSNSGA GDLIGTLGCD MFKVNSSTVP KLWPDNTFMF
LLAPFFHHGM GHVSKIRKFL GIPTVFNVLG PLLHPVSHVN KRILGVYSKE LAPEYAKAAA
LVYPGSETFI VWGHVGLDEV SPIGKTTVWH IDPTSSELKL KTFQLEPSMF GLEEHELSKC
ASYGPKENAR ILKEEVLSGK YHLGDNNPIY DYILMNTAVL YCLSQGHQNW KEGIIKAEES
IHSGNALRSL EHFIDSVSSL
