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Database: UniProt
Entry: A0A286EM54_9ACTN
LinkDB: A0A286EM54_9ACTN
Original site: A0A286EM54_9ACTN 
ID   A0A286EM54_9ACTN        Unreviewed;       265 AA.
AC   A0A286EM54;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Purine nucleoside phosphorylase {ECO:0000256|ARBA:ARBA00013834, ECO:0000256|PIRNR:PIRNR000477};
DE            EC=2.4.2.1 {ECO:0000256|ARBA:ARBA00011886, ECO:0000256|PIRNR:PIRNR000477};
DE   AltName: Full=Inosine-guanosine phosphorylase {ECO:0000256|PIRNR:PIRNR000477};
GN   ORFNames=SAMN05892883_1461 {ECO:0000313|EMBL:SOD72012.1};
OS   Jatrophihabitans sp. GAS493.
OC   Bacteria; Actinomycetota; Actinomycetes; Jatrophihabitantales;
OC   Jatrophihabitantaceae; Jatrophihabitans.
OX   NCBI_TaxID=1907575 {ECO:0000313|EMBL:SOD72012.1, ECO:0000313|Proteomes:UP000218903};
RN   [1] {ECO:0000313|EMBL:SOD72012.1, ECO:0000313|Proteomes:UP000218903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GAS493 {ECO:0000313|EMBL:SOD72012.1,
RC   ECO:0000313|Proteomes:UP000218903};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The purine nucleoside phosphorylases catalyze 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. Cleaves
CC       guanosine, inosine, 2'-deoxyguanosine and 2'-deoxyinosine.
CC       {ECO:0000256|ARBA:ARBA00002678}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a purine 2'-deoxy-D-ribonucleoside + phosphate = 2-deoxy-
CC         alpha-D-ribose 1-phosphate + a purine nucleobase;
CC         Xref=Rhea:RHEA:36431, ChEBI:CHEBI:26386, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57259, ChEBI:CHEBI:142361; EC=2.4.2.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001173};
CC   -!- PATHWAY: Purine metabolism; purine nucleoside salvage.
CC       {ECO:0000256|ARBA:ARBA00005058, ECO:0000256|PIRNR:PIRNR000477}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|ARBA:ARBA00011233}.
CC   -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family.
CC       {ECO:0000256|ARBA:ARBA00006751, ECO:0000256|PIRNR:PIRNR000477}.
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DR   EMBL; LT907982; SOD72012.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A286EM54; -.
DR   InParanoid; A0A286EM54; -.
DR   UniPathway; UPA00606; -.
DR   Proteomes; UP000218903; Chromosome i.
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; IPR011269; PUNP.
DR   InterPro; IPR011268; Purine_phosphorylase.
DR   InterPro; IPR018099; Purine_phosphorylase-2_CS.
DR   NCBIfam; TIGR01697; PNPH-PUNA-XAPA; 1.
DR   NCBIfam; TIGR01698; PUNP; 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   PIRSF; PIRSF000477; PurNPase; 1.
DR   SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
DR   PROSITE; PS01240; PNP_MTAP_2; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|PIRNR:PIRNR000477};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000477}.
FT   DOMAIN          27..263
FT                   /note="Nucleoside phosphorylase"
FT                   /evidence="ECO:0000259|Pfam:PF01048"
FT   BINDING         33
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         65
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         85..87
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         117
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         186
FT                   /ligand="a purine D-ribonucleoside"
FT                   /ligand_id="ChEBI:CHEBI:142355"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         205
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         228
FT                   /ligand="a purine D-ribonucleoside"
FT                   /ligand_id="ChEBI:CHEBI:142355"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
SQ   SEQUENCE   265 AA;  27428 MW;  9A1A4A26445E915C CRC64;
     MTTDPAPDAR AAADQLARLT GVDQHDVAIV LGSGWVPAVE ALGVATHEFP VTDLPGFLPP
     AVAGHAGRIR SLNVAGKRVL AFLGRTHLYE GRGVAPVVHG VRVAAAAGCK TVVLTNACGG
     LRPGMAVGDP VLISDHLNLT WQTPLLGPRF VDLTDVYSKR LRELMLSIDP SLTSGVYAMF
     HGPQYETPAE VRMAGILGAD LVGMSTVLEA IAAHAEGCSV LGLSLVTNLA AGITGEPLDH
     QEVLAAGLAA ATRMGGLLAE FIEKL
//
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