PNPH_PLAVS
ID PNPH_PLAVS Reviewed; 245 AA.
AC A5K9M4;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Purine nucleoside phosphorylase {ECO:0000303|PubMed:19575810};
DE EC=2.4.2.1 {ECO:0000269|PubMed:19575810};
DE AltName: Full=PvPNP {ECO:0000303|PubMed:19575810};
GN Name=PNP {ECO:0000303|PubMed:19575810};
GN ORFNames=PVX_080575 {ECO:0000312|EMBL:EDL44096.1};
OS Plasmodium vivax (strain Salvador I).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=126793 {ECO:0000312|Proteomes:UP000008333};
RN [1] {ECO:0000312|Proteomes:UP000008333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Salvador I {ECO:0000312|Proteomes:UP000008333};
RX PubMed=18843361; DOI=10.1038/nature07327;
RA Carlton J.M., Adams J.H., Silva J.C., Bidwell S.L., Lorenzi H., Caler E.,
RA Crabtree J., Angiuoli S.V., Merino E.F., Amedeo P., Cheng Q.,
RA Coulson R.M.R., Crabb B.S., del Portillo H.A., Essien K., Feldblyum T.V.,
RA Fernandez-Becerra C., Gilson P.R., Gueye A.H., Guo X., Kang'a S.,
RA Kooij T.W.A., Korsinczky M., Meyer E.V.-S., Nene V., Paulsen I., White O.,
RA Ralph S.A., Ren Q., Sargeant T.J., Salzberg S.L., Stoeckert C.J.,
RA Sullivan S.A., Yamamoto M.M., Hoffman S.L., Wortman J.R., Gardner M.J.,
RA Galinski M.R., Barnwell J.W., Fraser-Liggett C.M.;
RT "Comparative genomics of the neglected human malaria parasite Plasmodium
RT vivax.";
RL Nature 455:757-763(2008).
RN [2] {ECO:0007744|PDB:3EMV}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND SUBUNIT.
RX PubMed=19575810; DOI=10.1186/1472-6807-9-42;
RA Chaikuad A., Brady R.L.;
RT "Conservation of structure and activity in Plasmodium purine nucleoside
RT phosphorylases.";
RL BMC Struct. Biol. 9:42-42(2009).
CC -!- FUNCTION: As part of the purine salvage pathway, catalyzes 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 (PubMed:19575810). Preferentially acts on inosine and guanosine, and to
CC a lesser extent on 2'-deoxyinosine and 2'-deoxyguanosine
CC (PubMed:19575810). {ECO:0000269|PubMed:19575810}.
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:0000269|PubMed:19575810};
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:0000269|PubMed:19575810};
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:0000269|PubMed:19575810};
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:0000269|PubMed:19575810};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15.4 uM for inosine {ECO:0000269|PubMed:19575810};
CC KM=11.2 uM for guanosine {ECO:0000269|PubMed:19575810};
CC KM=61.4 uM for 2'-deoxyinosine {ECO:0000269|PubMed:19575810};
CC KM=35.1 uM for 2'-deoxyguanosine {ECO:0000269|PubMed:19575810};
CC Note=kcat is 1.2 sec(-1) with inosine as substrate (PubMed:19575810).
CC kcat is 0.7 sec(-1) with guanosine as substrate (PubMed:19575810).
CC kcat is 5.6 sec(-1) with 2'-deoxyinosine as substrate
CC (PubMed:19575810). kcat is 0.7 sec(-1) with 2'-deoxyguanosine as
CC substrate (PubMed:19575810). {ECO:0000269|PubMed:19575810};
CC -!- PATHWAY: Purine metabolism; purine nucleoside salvage.
CC {ECO:0000269|PubMed:19575810}.
CC -!- SUBUNIT: Homohexamer; trimer of homodimers.
CC {ECO:0000305|PubMed:19575810}.
CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family.
CC {ECO:0000305}.
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DR EMBL; AAKM01000011; EDL44096.1; -; Genomic_DNA.
DR RefSeq; XP_001613823.1; XM_001613773.1.
DR PDB; 3EMV; X-ray; 1.85 A; A=1-245.
DR PDBsum; 3EMV; -.
DR AlphaFoldDB; A5K9M4; -.
DR SMR; A5K9M4; -.
DR STRING; 126793.A5K9M4; -.
DR EnsemblProtists; EDL44096; EDL44096; PVX_080575.
DR GeneID; 5473095; -.
DR KEGG; pvx:PVX_080575; -.
DR VEuPathDB; PlasmoDB:PVX_080575; -.
DR InParanoid; A5K9M4; -.
DR OMA; MSDVFHL; -.
DR PhylomeDB; A5K9M4; -.
DR UniPathway; UPA00606; -.
DR EvolutionaryTrace; A5K9M4; -.
DR Proteomes; UP000008333; Chromosome 10.
DR Proteomes; UP000008333; Unassembled WGS sequence.
DR GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IDA:UniProtKB.
DR GO; GO:0006148; P:inosine catabolic process; IDA:UniProtKB.
DR GO; GO:0006195; P:purine nucleotide catabolic process; IDA:UniProtKB.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1580; -; 1.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; SSF53167; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Purine salvage; Reference proteome;
KW Transferase.
FT CHAIN 1..245
FT /note="Purine nucleoside phosphorylase"
FT /id="PRO_0000451827"
FT ACT_SITE 207
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8I3X4"
FT BINDING 8
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q8I3X4"
FT BINDING 24..28
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000305|PubMed:19575810,
FT ECO:0007744|PDB:3EMV"
FT BINDING 46
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q8I3X4"
FT BINDING 89..92
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000305|PubMed:19575810,
FT ECO:0007744|PDB:3EMV"
FT BINDING 184..185
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q8I3X4"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:3EMV"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:3EMV"
FT STRAND 18..24
FT /evidence="ECO:0007829|PDB:3EMV"
FT HELIX 26..33
FT /evidence="ECO:0007829|PDB:3EMV"
FT STRAND 36..45
FT /evidence="ECO:0007829|PDB:3EMV"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:3EMV"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:3EMV"
FT HELIX 69..81
FT /evidence="ECO:0007829|PDB:3EMV"
FT STRAND 86..96
FT /evidence="ECO:0007829|PDB:3EMV"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:3EMV"
FT STRAND 106..117
FT /evidence="ECO:0007829|PDB:3EMV"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:3EMV"
FT HELIX 133..145
FT /evidence="ECO:0007829|PDB:3EMV"
FT STRAND 151..159
FT /evidence="ECO:0007829|PDB:3EMV"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:3EMV"
FT HELIX 171..176
FT /evidence="ECO:0007829|PDB:3EMV"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:3EMV"
FT HELIX 186..196
FT /evidence="ECO:0007829|PDB:3EMV"
FT STRAND 199..208
FT /evidence="ECO:0007829|PDB:3EMV"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:3EMV"
FT HELIX 226..244
FT /evidence="ECO:0007829|PDB:3EMV"
SQ SEQUENCE 245 AA; 27223 MW; 7336069AD4A1BDA3 CRC64;
MEGEMQRHIK LTKAQTTPVV LVVGDPGRVD KVKVLCDSYV DLAYNREYKS VECTYKGQKF
LCVSHGVGSA GCAICFEELM NNGAKVIIRA GSCGSLQPTQ MKRGDICICN AAVREDRVSH
LMIYSDFPAV ADYEVYATLN QVAEELKVPV FNGISLSSDM YYPHKIIPTR LEDYSKANVA
VVEMEVATLM VMGTLRKVKT GGIFIVDGCP LKWDEGDFDN NLVPERLENM IKISLETCAR
LAKKY
