ID PUR1_STAAS Reviewed; 494 AA. AC Q6GAE3; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 119. DE RecName: Full=Amidophosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01931}; DE Short=ATase {ECO:0000255|HAMAP-Rule:MF_01931}; DE EC=2.4.2.14 {ECO:0000255|HAMAP-Rule:MF_01931}; DE AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_01931}; DE Short=GPATase {ECO:0000255|HAMAP-Rule:MF_01931}; DE Flags: Precursor; GN Name=purF {ECO:0000255|HAMAP-Rule:MF_01931}; GN OrderedLocusNames=SAS1006; OS Staphylococcus aureus (strain MSSA476). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=282459; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MSSA476; RX PubMed=15213324; DOI=10.1073/pnas.0402521101; RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z., RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N., RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A., RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M., RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.; RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence RT for the rapid evolution of virulence and drug resistance."; RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004). CC -!- FUNCTION: Catalyzes the formation of phosphoribosylamine from CC phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP- CC Rule:MF_01931}. 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01931}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01931}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01931}; 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. {ECO:0000255|HAMAP-Rule:MF_01931}. CC -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01931}. 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; BX571857; CAG42780.1; -; Genomic_DNA. DR RefSeq; WP_000483713.1; NC_002953.3. DR AlphaFoldDB; Q6GAE3; -. DR SMR; Q6GAE3; -. DR MEROPS; C44.001; -. DR KEGG; sas:SAS1006; -. DR HOGENOM; CLU_022389_3_1_9; -. DR UniPathway; UPA00074; UER00124. DR GO; GO:0004044; F:amidophosphoribosyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro. 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; PF13537; GATase_7; 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 3: Inferred from homology; KW Glutamine amidotransferase; Glycosyltransferase; Magnesium; Metal-binding; KW Purine biosynthesis; Transferase. FT PROPEP 1..10 FT /evidence="ECO:0000250" FT /id="PRO_0000045302" FT CHAIN 11..494 FT /note="Amidophosphoribosyltransferase" FT /id="PRO_0000045303" FT DOMAIN 11..231 FT /note="Glutamine amidotransferase type-2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931" FT ACT_SITE 11 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931" FT BINDING 294 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931" FT BINDING 356 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931" FT BINDING 357 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01931" SQ SEQUENCE 494 AA; 54397 MW; FED58A366B36AD8A CRC64; MFNYSGLNEE CGVFGIWNHP EAAQLTYMGL HSLQHRGQEG AGIVVSDQNE LKGERGLGLL TEAIKDDQME RLKGYQHAIG HVRYATSGNK GIENIQPFLY HFYDMSVGIC HNGNLINAKS LRQNLEKQGA IFHSSSDTEV IMHLIRRSKA PTFEEALKES LRKVKGGFTF AILTKDALYG AVDPNAIRPL VVGKMKDGTY ILASETCAID VLGAEFVQDI HAGEYVVIND KGITVKSYTH HTTTAISAME YIYFARPDST IAGKNVHAVR KASGKKLAQE SPVNADMVIG VPNSSLSAAS GYAEEIGLPY EMGLVKNQYV ARTFIQPTQE LREQGVRVKL SAVKDIVDGK NIILVDDSIV RGTTIRRIVK MLKDSGANKV HVRIASPEFM FPSFYGIDVS TTAELISASK SPEEIKDYIG ADSLAYLSVD GLIESIGLDY DAPYSGLCVE SFTGDYPAGL YDYEANYKAH LSHRQKQYIS KNKHFFDSEG NLNV //