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Database: UniProt
Entry: A0A2G8LD00_STIJA
LinkDB: A0A2G8LD00_STIJA
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ID   A0A2G8LD00_STIJA        Unreviewed;       253 AA.
AC   A0A2G8LD00;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
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=BSL78_04999 {ECO:0000313|EMBL:PIK58085.1};
OS   Stichopus japonicus (Sea cucumber).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC   Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX   NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK58085.1, ECO:0000313|Proteomes:UP000230750};
RN   [1] {ECO:0000313|EMBL:PIK58085.1, ECO:0000313|Proteomes:UP000230750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Shaxun {ECO:0000313|EMBL:PIK58085.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:PIK58085.1};
RX   PubMed=29023486;
RA   Zhang X., Sun L., Yuan J., Sun Y., Gao Y., Zhang L., Li S., Dai H.,
RA   Hamel J.F., Liu C., Yu Y., Liu S., Lin W., Guo K., Jin S., Xu P.,
RA   Storey K.B., Huan P., Zhang T., Zhou Y., Zhang J., Lin C., Li X., Xing L.,
RA   Huo D., Sun M., Wang L., Mercier A., Li F., Yang H., Xiang J.;
RT   "The sea cucumber genome provides insights into morphological evolution and
RT   visceral regeneration.";
RL   PLoS Biol. 15:E2003790-E2003790(2017).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PIK58085.1}.
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DR   EMBL; MRZV01000123; PIK58085.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G8LD00; -.
DR   STRING; 307972.A0A2G8LD00; -.
DR   UniPathway; UPA00606; -.
DR   Proteomes; UP000230750; 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; 2.
DR   InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR   InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR   InterPro; IPR011268; Purine_phosphorylase.
DR   PANTHER; PTHR11904; METHYLTHIOADENOSINE/PURINE NUCLEOSIDE PHOSPHORYLASE; 1.
DR   PANTHER; PTHR11904:SF9; PURINE NUCLEOSIDE PHOSPHORYLASE-RELATED; 1.
DR   Pfam; PF01048; PNP_UDP_1; 2.
DR   PIRSF; PIRSF000477; PurNPase; 2.
DR   SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000230750}.
FT   DOMAIN          31..168
FT                   /note="Nucleoside phosphorylase"
FT                   /evidence="ECO:0000259|Pfam:PF01048"
FT   DOMAIN          182..243
FT                   /note="Nucleoside phosphorylase"
FT                   /evidence="ECO:0000259|Pfam:PF01048"
SQ   SEQUENCE   253 AA;  27767 MW;  C401E1C4868CF9F5 CRC64;
     MSKEDTPYSY EQLEKFATII KEKTGSFHPS IGIIAGSGQG VLVEAVQNAI TIPYTDIEGF
     PQSTVAGHSG EFVVGKIGDK DVLVMSGRLH LYEGYPAWKL VAPIRVMSLL GIKTLIVCNA
     AGGINRDFKV GDFMLMKDHI GFPILAGQNP LRGPNDERWV LGWKHPWPAF AHGTGLLDWL
     CMSTVPEAIA ARHCGMEVLG MSMVTNACIM ENDIEQKTDH QEVLETGKRQ GESMCKLISK
     IVEKMDHKEQ NGA
//
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