ID A0A182T9P2_9DIPT Unreviewed; 302 AA.
AC A0A182T9P2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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};
OS Anopheles maculatus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles; Anopheles maculatus group.
OX NCBI_TaxID=74869 {ECO:0000313|EnsemblMetazoa:AMAM022459-PA, ECO:0000313|Proteomes:UP000075901};
RN [1] {ECO:0000313|Proteomes:UP000075901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=maculatus3 {ECO:0000313|Proteomes:UP000075901};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles maculatus species B.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMAM022459-PA}
RP IDENTIFICATION.
RC STRAIN=maculatus3 {ECO:0000313|EnsemblMetazoa:AMAM022459-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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 AlphaFoldDB; A0A182T9P2; -.
DR EnsemblMetazoa; AMAM022459-RA; AMAM022459-PA; AMAM022459.
DR VEuPathDB; VectorBase:AMAM022459; -.
DR OrthoDB; 5475828at2759; -.
DR UniPathway; UPA00606; -.
DR Proteomes; UP000075901; Unassembled WGS sequence.
DR GO; GO:0047975; F:guanosine phosphorylase activity; IEA:RHEA.
DR GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR CDD; cd09009; PNP-EcPNPII_like; 1.
DR Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR InterPro; IPR011270; Pur_Nuc_Pase_Ino/Guo-sp.
DR InterPro; IPR011268; Purine_phosphorylase.
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; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
PE 3: Inferred from homology;
FT DOMAIN 93..301
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 302 AA; 32713 MW; D01CA52CABDDACB0 CRC64;
MSKFSYLQNG NGVPNGVSNG AAPHANGHHH VQNGHSNVNR NGFDGLPAAE TYQQKAATSG
PFHMPRTEHG GYTYDTLQEI ANYLLERTEL RPKVGIICGS GLGTLADQLT DVDSFDYETI
PHFPVSTVAG HVGRLVFGYL AGVPVMCMQG RFHHYEGYPL AKCSMPVRVM HLIGCTHLIA
TNAAGGANPK YRVGDIMLIK DHINLMGFAG NNPLQGPNDE RFGPRFFGMA NTYDPKLNQT
AKVIARQIGI ENELREGVYT CLGGPNFETV AEVKMLAMLG VDAIGMSTVH EIITARHCGM
TC
//
