ID   PUR1_LACKL              Reviewed;         510 AA.
AC   Q12698;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Amidophosphoribosyltransferase;
DE            Short=ATase;
DE            EC=2.4.2.14;
DE   AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase;
GN   Name=ADE4;
OS   Lachancea kluyveri (Yeast) (Saccharomyces kluyveri).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=4934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IH404;
RA   Marsh L., Branda S.;
RL   Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. {ECO:0000305}.
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DR   EMBL; U32992; AAA75450.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q12698; -.
DR   SMR; Q12698; -.
DR   MEROPS; C44.001; -.
DR   UniPathway; UPA00074; UER00124.
DR   GO; GO:0004044; F:amidophosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..510
FT                   /note="Amidophosphoribosyltransferase"
FT                   /id="PRO_0000139645"
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"
SQ   SEQUENCE   510 AA;  57012 MW;  C3B3580B3F460378 CRC64;
     MCGILGIALA DQSSVVAPEL FDGSLFLQHR GQDAAGMATC GERGRLYQCK GNGMARDVFT
     QHRMSGLVGS MGIAHLRYPT AGSCANSEAQ PFYVNSPYGI CLSHNGTLVN TLSLRSYLDE
     VVHRHINTDS DSELLLNVFA AELERHNKYR VNNDDIFHAL EGVYRQCRGG YACVGMLAGY
     SLFGFRDPNG IRPLLFGERV NPDGTKDYML ASESVVLKAH NFNKFRDLKP GEAVIIPKDC
     NKQEPEFRQV VPTNSYRPDL FEYVYFARPD SVLDGISVYH TRLQMGIKLA ENVKKVVDPD
     EIDVVVSVPD TARTCALQCA NHLNKPYREA FVKNRYVGRT FIMPNQKERV SSVRRKLNPM
     DFEFKDKRVL IVDDSIVRGT TSKEIINMAK ESGATKVYFA SAAPAIRFNH IYGIDLADTK
     QLVAYNRTTD EVAQELGCEK VIYQSLEDLV DCCKTDKIDK FEVGVFTGNY VTGVEDGYLQ
     ELERVRALNK AKLTTAKAEV DIGLYNSADY