(data stored in SCRATCH zone)

SWISSPROT: Q75BS3_ASHGO

ID   Q75BS3_ASHGO            Unreviewed;       308 AA.
AC   Q75BS3;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 102.
DE   RecName: Full=Purine nucleoside phosphorylase {ECO:0000256|PIRNR:PIRNR000477};
DE            EC=2.4.2.1 {ECO:0000256|PIRNR:PIRNR000477};
DE   AltName: Full=Inosine-guanosine phosphorylase {ECO:0000256|PIRNR:PIRNR000477};
GN   ORFNames=AGOS_ACR198W {ECO:0000313|EMBL:AAS51424.1};
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:AAS51424.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS51424.1, 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   -!- FUNCTION: The purine nucleoside phosphorylases catalyze the
CC       phosphorolytic breakdown of the N-glycosidic bond in the beta-
CC       (deoxy)ribonucleoside molecules, with the formation of the
CC       corresponding free purine bases and pentose-1-phosphate.
CC       {ECO:0000256|PIRNR:PIRNR000477}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a purine D-ribonucleoside + phosphate = a purine nucleobase +
CC         alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:19805, ChEBI:CHEBI:26386,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57720, ChEBI:CHEBI:142355; EC=2.4.2.1;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000477};
CC   -!- PATHWAY: Purine metabolism; purine nucleoside salvage.
CC       {ECO:0000256|PIRNR:PIRNR000477}.
CC   -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family.
CC       {ECO:0000256|PIRNR:PIRNR000477}.
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DR   EMBL; AE016816; AAS51424.1; -; Genomic_DNA.
DR   RefSeq; NP_983600.1; NM_208953.1.
DR   STRING; 33169.AAS51424; -.
DR   EnsemblFungi; AAS51424; AAS51424; AGOS_ACR198W.
DR   GeneID; 4619732; -.
DR   KEGG; ago:AGOS_ACR198W; -.
DR   HOGENOM; HOG000045183; -.
DR   InParanoid; Q75BS3; -.
DR   KO; K03783; -.
DR   OMA; EGVYAQF; -.
DR   UniPathway; UPA00606; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0047724; F:inosine nucleosidase activity; IEA:EnsemblFungi.
DR   GO; GO:0070635; F:nicotinamide riboside hydrolase activity; IEA:EnsemblFungi.
DR   GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IBA:GO_Central.
DR   GO; GO:0046115; P:guanosine catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0006148; P:inosine catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0034356; P:NAD biosynthesis via nicotinamide riboside salvage pathway; IEA:EnsemblFungi.
DR   GO; GO:0019358; P:nicotinate nucleotide salvage; IEA:EnsemblFungi.
DR   Gene3D; 3.40.50.1580; -; 1.
DR   InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR   InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR   InterPro; IPR011268; Purine_phosphorylase.
DR   PANTHER; PTHR11904; PTHR11904; 1.
DR   Pfam; PF01048; PNP_UDP_1; 1.
DR   PIRSF; PIRSF000477; PurNPase; 1.
DR   SUPFAM; SSF53167; SSF53167; 1.
DR   TIGRFAMs; TIGR01697; PNPH-PUNA-XAPA; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q75BS3.
DR   SWISS-2DPAGE; Q75BS3.
KW   Glycosyltransferase {ECO:0000256|PIRNR:PIRNR000477};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000477}.
FT   DOMAIN          38..305
FT                   /note="PNP_UDP_1"
FT                   /evidence="ECO:0000259|Pfam:PF01048"
FT   REGION          98..100
FT                   /note="Phosphate binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         44
FT                   /note="Phosphate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         78
FT                   /note="Phosphate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         131
FT                   /note="Phosphate; via amide nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         216
FT                   /note="Purine nucleoside"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         235
FT                   /note="Phosphate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         258
FT                   /note="Purine nucleoside"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
SQ   SEQUENCE   308 AA;  32717 MW;  2B26D6BD7E0BE51A CRC64;
     MASFDINQER AVIQDAAEFL NGEITAHFGA TCEFKPRVLI ICGSGLGGIS HVISSNPQPL
     SVPYSAIPGF KASTIVGHAG DLLFGFMNKT PVVLMKGRLH GYEGNTAQEI TRPIRILNEL
     GSIGVLVVTN AAGAVNPEFS ACELMCINDH ISFPGLCGFH PLRGPNFDET GPRFLATSDA
     YDLKLRQLLF SKHKELGIAR RLHEGVYAHV SGPTFESRAE SRLIRLVGAD CVGMSTVPEV
     VVARHCGWRV LALSLITNCV VLSPAASALD TNPVPLDLGK AEHSEVIVNA AAASADVEQL
     VEAVVGAL
//

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