(data stored in SCRATCH zone)

SWISSPROT: Q4WD74_ASPFU

ID   Q4WD74_ASPFU            Unreviewed;       583 AA.
AC   Q4WD74;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 100.
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=AFUA_6G03750 {ECO:0000313|EMBL:EAL85664.1};
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL85664.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL85664.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAL85664.1}.
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DR   EMBL; AAHF01000012; EAL85664.1; -; Genomic_DNA.
DR   RefSeq; XP_747702.1; XM_742609.1.
DR   STRING; 746128.CADAFUBP00009190; -.
DR   MEROPS; C44.001; -.
DR   EnsemblFungi; EAL85664; EAL85664; AFUA_6G03750.
DR   GeneID; 3505068; -.
DR   KEGG; afm:AFUA_6G03750; -.
DR   EuPathDB; FungiDB:Afu6g03750; -.
DR   HOGENOM; HOG000033687; -.
DR   InParanoid; Q4WD74; -.
DR   KO; K00764; -.
DR   OMA; KGPQDAC; -.
DR   OrthoDB; 400911at2759; -.
DR   UniPathway; UPA00074; UER00124.
DR   Proteomes; UP000002530; Chromosome 6.
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; Q4WD74.
DR   SWISS-2DPAGE; Q4WD74.
KW   Glycosyltransferase {ECO:0000256|PIRNR:PIRNR000485,
KW   ECO:0000313|EMBL:EAL85664.1}; 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:UP000002530};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000485, ECO:0000313|EMBL:EAL85664.1}.
FT   DOMAIN          2..241
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           313
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000485-2"
FT   METAL           375
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000485-2"
FT   METAL           376
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000485-2"
SQ   SEQUENCE   583 AA;  64043 MW;  A366F6A05F2D6F46 CRC64;
     MCGIIGLILA NPKSSAAVDL HEALYLLQHR GQDAAGIATC AAGGRIYQLK ANGMAAKVFN
     DGARVADLPG FMGIGHLRYP TAGSSANAEA QPFYVNSPYG ICLAHNGNLI NAPELKRYLD
     LEAHRHINTD SDSELMLNIF ADELSETKKA RVNREDLFAS LSRMYERCQG GWACTAMLAG
     FGILGFRDSY GIRPLVLGSR PSLDGPGTDY MMASESVALH QLGFSNFRDI QPGEAVIIEK
     GGEPVFRQVA PKKAYAPDIF EYVYFARPDS VIDGISVYRS RQRMGDRLAA RILDVLGPEI
     VKDIDVVIPI PETSTTSAAA VARYLDKPYC QGFVKNRYVF RTFIMPEQKT RQKGVRRKLN
     AMQAEFKDRN VLLVDDSIVR GTTSREIVTM AREAGAKKVY FASCAPEITH AHVYGIDLAS
     PSELVAHGRD ANSIARHIGA DSVIFQTLDD LIGACAEITK ENGLSEPVNF EVGVFCGNYI
     TPIDDGYFDH LEKIRGEGRK IKAVDRAKEA VTHGFANEED YQIAANGVKL DQHGKIVPAK
     YPGESEVLQA GFNRCNKPMT HEEEPPKVKD RMDISIHNIA DHE
//

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