(data stored in SCRATCH zone)

SWISSPROT: C5DD99_LACTC

ID   C5DD99_LACTC            Unreviewed;       510 AA.
AC   C5DD99;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 67.
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   OrderedLocusNames=KLTH0B09460g {ECO:0000313|EMBL:CAR21760.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21760.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR21760.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P.,
RA   Jubin C., Poulain J., Barbe V., Segurens B., Artiguenave F.,
RA   Anthouard V., Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R.,
RA   Durrens P., Jean G., Marck C., Martin T., Nikolski M., Rolland T.,
RA   Seret M.-L., Casaregola S., Despons L., Fairhead C., Fischer G.,
RA   Lafontaine I., Leh V., Lemaire M., de Montigny J., Neuveglise C.,
RA   Thierry A., Blanc-Lenfle I., Bleykasten C., Diffels J., Fritsch E.,
RA   Frangeul L., Goeffon A., Jauniaux N., Kachouri-Lafond R., Payen C.,
RA   Potier S., Pribylova L., Ozanne C., Richard G.-F., Sacerdot C.,
RA   Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
CC         = 5-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.
CC       {ECO:0000256|PIRSR:PIRSR000485-2};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-
CC       ribose 1-diphosphate: step 1/2. {ECO:0000256|PIRNR:PIRNR000485}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       purine/pyrimidine phosphoribosyltransferase family.
CC       {ECO:0000256|PIRNR:PIRNR000485}.
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DR   EMBL; CU928166; CAR21760.1; -; Genomic_DNA.
DR   RefSeq; XP_002552198.1; XM_002552152.1.
DR   STRING; 381046.XP_002552198.1; -.
DR   MEROPS; C44.001; -.
DR   EnsemblFungi; CAR21760; CAR21760; KLTH0B09460g.
DR   GeneID; 8291041; -.
DR   KEGG; lth:KLTH0B09460g; -.
DR   HOGENOM; HOG000033687; -.
DR   InParanoid; C5DD99; -.
DR   KO; K00764; -.
DR   OMA; FRPLCLG; -.
DR   OrthoDB; 400911at2759; -.
DR   UniPathway; UPA00074; UER00124.
DR   Proteomes; UP000002036; Chromosome B.
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; 3.60.20.10; -; 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; C5DD99.
DR   SWISS-2DPAGE; C5DD99.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002036};
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:UP000002036};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000485}.
FT   DOMAIN        2    239       Glutamine amidotransferase type-2.
FT                                {ECO:0000259|PROSITE:PS51278}.
FT   ACT_SITE      2      2       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR000485-1}.
FT   METAL       311    311       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR000485-2}.
FT   METAL       373    373       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR000485-2}.
FT   METAL       374    374       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR000485-2}.
SQ   SEQUENCE   510 AA;  56433 MW;  FBF27EACF695DC20 CRC64;
     MCGVLGIALG DQTSAVAPEL FDGCLFLQHR GQDAAGIATC GQRGRLYQCK GNGMARDVFT
     QQRMANLVGS MGIAHLRYPT AGSSANSEAQ PFYVNSPYGI LLGHNGNLVN TLSLRRYMDE
     DVHRHINTDS DSELLLNILA AELEKHNKYR VNNDDIFHAL EGVYRLCRGG YACVGMLAGY
     AMIGFRDPNG IRPLLFGERT RPDGTKDYML ASESVVLKAH NFNNFRDLAP GEAVIVPKDC
     GNTAPEFKQV VPINSYRPDL FEYVYFARPD SVLDGISVYH TRLAMGVKLA ESIRKEIDPN
     DIDVVVSVPD TARTCALQCA NTLQIPYREG FVKNRYVGRT FIMPNQKERV SSVRRKLNAM
     DSEFKGKRVL VVDDSIVRGT TSKEIISMAK EAGASKVYFA SAAPAIRYNH IYGIDLADTK
     QLVAFDKSTE EVSQELGCDR VFYQSLEDLV DCCKTDKISK FEVGVFTGNY VTGVEDGYLQ
     ELEKVRALNA AKQNFAKADS DIGLYNSADF
//

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