(data stored in ACNUC7421 zone)

SWISSPROT: Q751N1_ASHGO

ID   Q751N1_ASHGO            Unreviewed;       510 AA.
AC   Q751N1;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 122.
DE   RecName: Full=Amidophosphoribosyltransferase {ECO:0000256|PIRNR:PIRNR000485};
DE            Short=ATase {ECO:0000256|PIRNR:PIRNR000485};
DE            EC=2.4.2.14 {ECO:0000256|PIRNR:PIRNR000485};
DE   AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase {ECO:0000256|PIRNR:PIRNR000485};
GN   ORFNames=AGOS_AGL334W {ECO:0000313|EMBL:AAS54157.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS54157.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54157.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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         Evidence={ECO:0000256|PIRNR:PIRNR000485};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000485-2};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR000485-2};
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:0000256|PIRNR:PIRNR000485}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. {ECO:0000256|PIRNR:PIRNR000485}.
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DR   EMBL; AE016820; AAS54157.1; -; Genomic_DNA.
DR   RefSeq; NP_986333.1; NM_211395.1.
DR   STRING; 33169.AAS54157; -.
DR   MEROPS; C44.001; -.
DR   EnsemblFungi; AAS54157; AAS54157; AGOS_AGL334W.
DR   GeneID; 4622626; -.
DR   KEGG; ago:AGOS_AGL334W; -.
DR   HOGENOM; HOG000033687; -.
DR   InParanoid; Q751N1; -.
DR   KO; K00764; -.
DR   OMA; KGPQDAC; -.
DR   UniPathway; UPA00074; UER00124.
DR   Proteomes; UP000000591; Chromosome VII.
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:0009116; P:nucleoside metabolic process; IEA:InterPro.
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.
PE   3: Inferred from homology;
DR   PRODOM; Q751N1.
DR   SWISS-2DPAGE; Q751N1.
KW   Glycosyltransferase {ECO:0000256|PIRNR:PIRNR000485};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000485-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000485-2};
KW   Purine biosynthesis {ECO:0000256|PIRNR:PIRNR000485};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000485}.
FT   DOMAIN          2..239
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   ACT_SITE        2
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000485-1"
FT   METAL           311
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000485-2"
FT   METAL           373
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000485-2"
FT   METAL           374
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000485-2"
SQ   SEQUENCE   510 AA;  56646 MW;  137D956EB534E6C6 CRC64;
     MCGILGVVLA DQSKVVAPEL FDGSLFLQHR GQDAAGIATC GPGGRLYQCK GNGMARDVFT
     QARMSGLVGS MGIAHLRYPT AGSSANSEAQ PFYVNSPYGI CMSHNGNLVN TMSLRRYLDE
     DVHRHINTDS DSELLLNIFA AELEKYNKYR VNNDDIFCAL EGVYKRCRGG YACVGMLAGY
     GLFGFRDPNG IRPLLFGERV NDDGTMDYML ASESVVLKAH RFQNIRDILP GQAVIIPKTC
     GSSPPEFRQV VPIEAYKPDL FEYVYFARAD SVLDGISVYH TRLLMGIKLA ENIKKQIDLD
     EIDVVVSVPD TARTCALECA NHLNKPYREG FVKNRYVGRT FIMPNQKERV SSVRRKLNPM
     NSEFKDKRVL IVDDSIVRGT TSKEIVNMAK ESGAAKVYFA SAAPAIRFNH IYGIDLADTK
     QLVAYNRTVE EITAELGCDR VIYQSLDDLI DCCKTDIISE FEVGVFTGNY VTGVEDVYLQ
     ELERCRALNN SNKGEAKAEV DIGLYNSADY
//

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