PUR1_STAAW
ID PUR1_STAAW Reviewed; 494 AA.
AC Q8NX91;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 124.
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}; OrderedLocusNames=MW0953;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
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;
CC Evidence={ECO:0000255|HAMAP-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; BA000033; BAB94818.1; -; Genomic_DNA.
DR RefSeq; WP_000483713.1; NC_003923.1.
DR AlphaFoldDB; Q8NX91; -.
DR SMR; Q8NX91; -.
DR MEROPS; C44.001; -.
DR EnsemblBacteria; BAB94818; BAB94818; BAB94818.
DR KEGG; sam:MW0953; -.
DR HOGENOM; CLU_022389_3_1_9; -.
DR OMA; ENAQPTF; -.
DR UniPathway; UPA00074; UER00124.
DR Proteomes; UP000000418; Chromosome.
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; -; 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; PF13537; GATase_7; 1.
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 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_0000029267"
FT CHAIN 11..494
FT /note="Amidophosphoribosyltransferase"
FT /id="PRO_0000029268"
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
