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Database: UniProt
Entry: T0U3V3_9STRE
LinkDB: T0U3V3_9STRE
Original site: T0U3V3_9STRE 
ID   T0U3V3_9STRE            Unreviewed;       269 AA.
AC   T0U3V3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Purine nucleoside phosphorylase {ECO:0000256|PIRNR:PIRNR000477};
DE            EC=2.4.2.1 {ECO:0000256|PIRNR:PIRNR000477};
DE   AltName: Full=Inosine-guanosine phosphorylase {ECO:0000256|PIRNR:PIRNR000477};
GN   ORFNames=HSISM1_1125 {ECO:0000313|EMBL:EQC77922.1};
OS   Streptococcus sp. HSISM1.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1316408 {ECO:0000313|EMBL:EQC77922.1};
RN   [1] {ECO:0000313|EMBL:EQC77922.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HSISM1 {ECO:0000313|EMBL:EQC77922.1};
RA   Van den Bogert B., Boekhorst J., Herrmann R., Smid E.J., Zoetendal E.G.,
RA   Kleerebezem M.;
RT   "Comparative Genomics Analysis of Streptococcus Isolates from the Human
RT   Small Intestine Reveals their Adaptation to a Highly Dynamic Ecosystem.";
RL   PLoS ONE 8:E83418-E83418(2013).
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.
CC       {ECO:0000256|PIRNR:PIRNR000477}.
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}.
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:EQC77922.1}.
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DR   EMBL; ASKI01000025; EQC77922.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0U3V3; -.
DR   PATRIC; fig|1316408.3.peg.629; -.
DR   eggNOG; COG0005; Bacteria.
DR   HOGENOM; CLU_054456_1_3_9; -.
DR   UniPathway; UPA00606; -.
DR   Proteomes; UP000015933; Chromosome.
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   InterPro; IPR018099; Purine_phosphorylase-2_CS.
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   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   ECO:0000313|EMBL:EQC77922.1};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000477, ECO:0000313|EMBL:EQC77922.1}.
FT   DOMAIN          24..267
FT                   /note="Nucleoside phosphorylase"
FT                   /evidence="ECO:0000259|Pfam:PF01048"
FT   BINDING         30
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         61
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         81..83
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         113
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         191
FT                   /ligand="a purine D-ribonucleoside"
FT                   /ligand_id="ChEBI:CHEBI:142355"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         210
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         233
FT                   /ligand="a purine D-ribonucleoside"
FT                   /ligand_id="ChEBI:CHEBI:142355"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
SQ   SEQUENCE   269 AA;  28689 MW;  A881FF1FB51558FF CRC64;
     MTLLAKINET AAFLKGKGME APEFGLILGS GLGELAEEIE NPVVVDYSEI PNWGRSTVVG
     HAGKLVYGEL AGRKVLALQG RFHFYEGNPL EVVTFPVRVM KVLGCEGVLV TNAAGGIGFG
     PGTLMAITDH INMTGKNPLI GENLDDFGPR FPDMSKAYTP EYRETAHKAA DKLGIKLDDG
     VYIGVTGPTY ETPAEIRAFK TLGADAVGMS TVPEVIIAAH SGLKVLGISC ITNFAAGFQE
     ELNHEEVVEV TERVKGDFKG LLKAILAEL
//
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