ID U4UD54_DENPD Unreviewed; 646 AA.
AC U4UD54;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Purine nucleoside phosphorylase {ECO:0000256|ARBA:ARBA00013834};
DE EC=2.4.2.1 {ECO:0000256|ARBA:ARBA00011886};
DE AltName: Full=Inosine phosphorylase {ECO:0000256|ARBA:ARBA00033072};
DE AltName: Full=Inosine-guanosine phosphorylase {ECO:0000256|ARBA:ARBA00031036};
DE Flags: Fragment;
GN ORFNames=D910_05233 {ECO:0000313|EMBL:ERL87845.1};
OS Dendroctonus ponderosae (Mountain pine beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Dendroctonus.
OX NCBI_TaxID=77166 {ECO:0000313|EMBL:ERL87845.1, ECO:0000313|Proteomes:UP000030742};
RN [1] {ECO:0000313|EMBL:ERL87845.1, ECO:0000313|Proteomes:UP000030742}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA Birol I., Jones S.J., Bohlmann J.;
RT "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT a major forest pest.";
RL Genome Biol. 14:R27-R27(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyguanosine + phosphate = 2-deoxy-alpha-D-ribose 1-
CC phosphate + guanine; Xref=Rhea:RHEA:27738, ChEBI:CHEBI:16235,
CC ChEBI:CHEBI:17172, ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00023929};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyinosine + phosphate = 2-deoxy-alpha-D-ribose 1-
CC phosphate + hypoxanthine; Xref=Rhea:RHEA:27750, ChEBI:CHEBI:17368,
CC ChEBI:CHEBI:28997, ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00023950};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine + phosphate = alpha-D-ribose 1-phosphate + guanine;
CC Xref=Rhea:RHEA:13233, ChEBI:CHEBI:16235, ChEBI:CHEBI:16750,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00023970};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=inosine + phosphate = alpha-D-ribose 1-phosphate +
CC hypoxanthine; Xref=Rhea:RHEA:27646, ChEBI:CHEBI:17368,
CC ChEBI:CHEBI:17596, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00023918};
CC -!- PATHWAY: Purine metabolism; purine nucleoside salvage.
CC {ECO:0000256|ARBA:ARBA00005058}.
CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006751}.
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DR EMBL; KB632003; ERL87845.1; -; Genomic_DNA.
DR AlphaFoldDB; U4UD54; -.
DR STRING; 77166.U4UD54; -.
DR UniPathway; UPA00606; -.
DR Proteomes; UP000030742; Unassembled WGS sequence.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR CDD; cd01824; Phospholipase_B_like; 1.
DR CDD; cd09009; PNP-EcPNPII_like; 1.
DR Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1.
DR Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR InterPro; IPR001087; GDSL.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR InterPro; IPR035547; Phospholipase_B.
DR InterPro; IPR011270; Pur_Nuc_Pase_Ino/Guo-sp.
DR InterPro; IPR011268; Purine_phosphorylase.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR NCBIfam; TIGR01700; PNPH; 1.
DR NCBIfam; TIGR01697; PNPH-PUNA-XAPA; 1.
DR PANTHER; PTHR11904; METHYLTHIOADENOSINE/PURINE NUCLEOSIDE PHOSPHORYLASE; 1.
DR PANTHER; PTHR11904:SF9; PURINE NUCLEOSIDE PHOSPHORYLASE-RELATED; 1.
DR Pfam; PF00657; Lipase_GDSL; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
DR SUPFAM; SSF52266; SGNH hydrolase; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000030742}.
FT DOMAIN 385..639
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ERL87845.1"
SQ SEQUENCE 646 AA; 71651 MW; 5B7B29795D4CB4C8 CRC64;
KRQQGPQGAQ FPCSHRDLPA RSQTRPQSVH QLRPGDIDVV GAIGDSLTAG FGVEVDSLLA
LLHEARGSSF SIGGAGTWQT HLTLPNILKQ FNPHLYGYSL NAITTDGKSK FNVAEGGAIS
NDMPFMARVL VDRIKRDKHV DLENDWKMIS VFIGHNDLCS DACYKRDFQK VLANHEADML
ETLRTFRNHL PRTVINLIPP IHLKILLDMT DKPASCIVPH IISCPCLIGL PHRHLVPQMM
RLMDQWQALD LQIANYPEFD SDQFTIIAHK FTLNFTLPRL KNGGMDYGYT AADCFHASQR
GHAKVSLALY AQLRKTKFNL KYPLDSDCYR LVIIRLAILT SPQSIAVSGT EQLVEMSALP
ADEFNRGFIE ESARFIRSRV PVAPKLLIIC GSGLGGLADT LEKPVTLSYD EIPNFPQSTV
PGHAGELIFG TLANVPVACM KGRFHYYEGY SLQKVTTPIR IMQLLGIKGL IVTNAAGSVN
KAYQVGDIML IKDHLNFFAF GGRHPLRGPN DPQFGARFFP MNRAYDRALL QVGKRAAAEV
GLANHCHEGV YGIYSGPNYE TVAEIKYLQL VGVDAIGMST VPEVLVAKHC GLRVFGFSFI
TNKCVDSYEE AEEPNHAHIL DVVQAKAEKL KNLVIKFVEH TSAQWL
//
