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Database: UniProt
Entry: A0A0M3K5X6_ANISI
LinkDB: A0A0M3K5X6_ANISI
Original site: A0A0M3K5X6_ANISI 
ID   A0A0M3K5X6_ANISI        Unreviewed;       364 AA.
AC   A0A0M3K5X6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=purine-nucleoside phosphorylase {ECO:0000256|ARBA:ARBA00011886};
DE            EC=2.4.2.1 {ECO:0000256|ARBA:ARBA00011886};
DE   AltName: Full=Inosine-guanosine phosphorylase {ECO:0000256|ARBA:ARBA00031036};
GN   ORFNames=ASIM_LOCUS15774 {ECO:0000313|EMBL:VDK56004.1};
OS   Anisakis simplex (Herring worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Anisakidae; Anisakis;
OC   Anisakis simplex complex.
OX   NCBI_TaxID=6269 {ECO:0000313|Proteomes:UP000036680, ECO:0000313|WBParaSite:ASIM_0001636701-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:ASIM_0001636701-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDK56004.1, ECO:0000313|Proteomes:UP000267096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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; UYRR01032548; VDK56004.1; -; Genomic_DNA.
DR   WBParaSite; ASIM_0001636701-mRNA-1; ASIM_0001636701-mRNA-1; ASIM_0001636701.
DR   UniPathway; UPA00606; -.
DR   Proteomes; UP000036680; Unplaced.
DR   Proteomes; UP000267096; Unassembled WGS sequence.
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; IPR011268; Purine_phosphorylase.
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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000267096}.
FT   DOMAIN          112..293
FT                   /note="Nucleoside phosphorylase"
FT                   /evidence="ECO:0000259|Pfam:PF01048"
SQ   SEQUENCE   364 AA;  40201 MW;  BC5CECB4B29F38F3 CRC64;
     MSTCCPAKSD QINKILRIRP IRKIQTCSFS LRFDPSGLER ADEKQSSEYI RDMINNMIAE
     SVLTLAEEFR NELFPLVTSM ISAKTFSPQC YEDLEKVANA IKSKVNLKET PTLAIICGSG
     LGDLAESVTD KQILPYSEIP GFPSTKVVGH KGNLVFGYLG GKYVMCVQGR FHPYEHGMNL
     ALGAMPVRIM HFLGVTKLVV SNAAGGLNEH FKQGDIMVIK DQLCLPALAG FSPFVGAHDE
     RFGARFPSMH AAYDPPLRKK AMEIAKQQGI RAFEGVYCMC AGPQYESPAE VNFRNVNLSR
     SGCGKTTWND GVWHFSNHQY VCCFTIANMD SDSTAEVAHT EVLDTAKEAS SRVCNFVAEV
     IKIM
//
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