PUR1_YEAST
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 03-AUG-2022, entry version 210.
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; 144.
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; P04046; -.
DR PRIDE; P04046; -.
DR EnsemblFungi; YMR300C_mRNA; YMR300C; YMR300C.
DR GeneID; 855346; -.
DR KEGG; sce:YMR300C; -.
DR SGD; S000004915; ADE4.
DR VEuPathDB; FungiDB:YMR300C; -.
DR eggNOG; KOG0572; Eukaryota.
DR HOGENOM; CLU_022389_2_1_1; -.
DR InParanoid; P04046; -.
DR OMA; ENAQPTF; -.
DR BioCyc; MetaCyc:YMR300C-MON; -.
DR BioCyc; YEAST:YMR300C-MON; -.
DR UniPathway; UPA00074; UER00124.
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; -; 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 Pfam; PF00156; Pribosyltran; 1.
DR PIRSF; PIRSF000485; Amd_phspho_trans; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR01134; purF; 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
