ID PUR1_YEAST Reviewed; 510 AA. AC P04046; D6W0C7; DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 2. DT 27-MAR-2024, entry version 216. DE RecName: Full=Amidophosphoribosyltransferase; DE Short=ATase; DE EC=2.4.2.14; DE AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase; GN Name=ADE4; OrderedLocusNames=YMR300C; ORFNames=YM9952.02C; 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=6376509; DOI=10.1016/s0021-9258(17)39755-7; RA Maentsaelae P., Zalkin H.; RT "Glutamine nucleotide sequence of Saccharomyces cerevisiae ADE4 encoding RT phosphoribosylpyrophosphate amidotransferase."; RL J. Biol. Chem. 259:8478-8484(1984). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169872; RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."; RL Nature 387:90-93(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 1-14. RA Lahti R., Glumoff V., Haemaelaeinen H., Paerssinen R., Maentsaelae P.; RT "Deletion analysis of the 5' flanking region of yeast ADE4 gene."; RL Eur. Congr. Biotechnol. 1:420-423(1987). 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 -!- CATALYTIC ACTIVITY: CC Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5- CC phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine; CC Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359, CC ChEBI:CHEBI:58681; EC=2.4.2.14; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=Binds 1 Mg(2+) ion per subunit.; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)- CC (5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1- CC diphosphate: step 1/2. CC -!- MISCELLANEOUS: Present with 18700 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; K02203; AAA34403.1; -; Genomic_DNA. DR EMBL; M57633; AAA34405.1; -; Genomic_DNA. DR EMBL; M74309; AAA34404.1; -; Genomic_DNA. DR EMBL; Z49212; CAA89133.1; -; Genomic_DNA. DR EMBL; BK006946; DAA10201.1; -; Genomic_DNA. DR PIR; S53970; S53970. DR RefSeq; NP_014029.1; NM_001182809.1. DR AlphaFoldDB; P04046; -. DR SMR; P04046; -. DR BioGRID; 35480; 151. DR DIP; DIP-6727N; -. DR IntAct; P04046; 11. DR MINT; P04046; -. DR STRING; 4932.YMR300C; -. DR MEROPS; C44.001; -. DR iPTMnet; P04046; -. DR MaxQB; P04046; -. DR PaxDb; 4932-YMR300C; -. DR PeptideAtlas; P04046; -. DR EnsemblFungi; YMR300C_mRNA; YMR300C; YMR300C. DR GeneID; 855346; -. DR KEGG; sce:YMR300C; -. DR AGR; SGD:S000004915; -. DR SGD; S000004915; ADE4. DR VEuPathDB; FungiDB:YMR300C; -. DR eggNOG; KOG0572; Eukaryota. DR HOGENOM; CLU_022389_2_1_1; -. DR InParanoid; P04046; -. DR OMA; IRHFGVK; -. DR OrthoDB; 4975at2759; -. DR BioCyc; MetaCyc:YMR300C-MONOMER; -. DR BioCyc; YEAST:YMR300C-MONOMER; -. DR UniPathway; UPA00074; UER00124. DR BioGRID-ORCS; 855346; 2 hits in 10 CRISPR screens. DR PHI-base; PHI:502; -. DR PRO; PR:P04046; -. DR Proteomes; UP000002311; Chromosome XIII. DR RNAct; P04046; Protein. DR GO; GO:0005737; C:cytoplasm; HDA:SGD. DR GO; GO:0004044; F:amidophosphoribosyltransferase activity; IDA:SGD. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IMP:SGD. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central. DR CDD; cd00715; GPATase_N; 1. DR CDD; cd06223; PRTases_typeI; 1. DR Gene3D; 3.40.50.2020; -; 1. DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1. DR HAMAP; MF_01931; PurF; 1. DR InterPro; IPR017932; GATase_2_dom. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR InterPro; IPR005854; PurF. DR InterPro; IPR035584; PurF_N. DR NCBIfam; TIGR01134; purF; 1. DR PANTHER; PTHR11907; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1. DR PANTHER; PTHR11907:SF0; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1. DR Pfam; PF13522; GATase_6; 1. DR Pfam; PF00156; Pribosyltran; 1. DR PIRSF; PIRSF000485; Amd_phspho_trans; 1. DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1. DR SUPFAM; SSF53271; PRTase-like; 1. DR PROSITE; PS51278; GATASE_TYPE_2; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 1: Evidence at protein level; KW Glutamine amidotransferase; Glycosyltransferase; Magnesium; Metal-binding; KW Purine biosynthesis; Reference proteome; Transferase. FT CHAIN 1..510 FT /note="Amidophosphoribosyltransferase" FT /id="PRO_0000139647" FT DOMAIN 2..239 FT /note="Glutamine amidotransferase type-2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609" FT ACT_SITE 2 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609" FT BINDING 373 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 374 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT CONFLICT 46..47 FT /note="IY -> VC (in Ref. 1; AAA34403/AAA34404)" FT /evidence="ECO:0000305" FT CONFLICT 62 FT /note="Missing (in Ref. 1; AAA34403/AAA34404)" FT /evidence="ECO:0000305" FT CONFLICT 82..87 FT /note="GSSANS -> PLRLIL (in Ref. 1)" FT /evidence="ECO:0000305" FT CONFLICT 156..158 FT /note="VFH -> GFSN (in Ref. 1; AAA34403/AAA34404)" FT /evidence="ECO:0000305" FT CONFLICT 234 FT /note="V -> G (in Ref. 1; AAA34403/AAA34404)" FT /evidence="ECO:0000305" FT CONFLICT 291 FT /note="E -> Q (in Ref. 1; AAA34403/AAA34404)" FT /evidence="ECO:0000305" SQ SEQUENCE 510 AA; 56719 MW; 1FE7A6F5B7C96710 CRC64; MCGILGIVLA NQTTPVAPEL CDGCIFLQHR GQDAAGIATC GSRGRIYQCK GNGMARDVFT QQRVSGLAGS MGIAHLRYPT AGSSANSEAQ PFYVNSPYGI NLAHNGNLVN TASLKRYMDE DVHRHINTDS DSELLLNIFA AELEKHNKYR VNNEDVFHAL EGVYRLCRGG YACVGLLAGF ALFGFRDPNG IRPLLFGERE NPDGTKDYML ASESVVFKAH NFTKYRDLKP GEAVIIPKNC SKGEPEFKQV VPINSYRPDL FEYVYFARPD SVLDGISVYH TRLAMGSKLA ENILKQLKPE DIDVVIPVPD TARTCALECA NVLGKPYREG FVKNRYVGRT FIMPNQRERV SSVRRKLNPM ESEFKGKKVL IVDDSIVRGT TSKEIVNMAK ESGATKVYFA SAAPAIRYNH IYGIDLTDTK NLIAYNRTDE EVAEVIGCER VIYQSLEDLI DCCKTDKITK FEDGVFTGNY VTGVEDGYIQ ELEEKRESIA NNSSDMKAEV DIGLYNCADY //