ID   DEOD_STRTR              Reviewed;         216 AA.
AC   Q56037;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   24-JAN-2024, entry version 79.
DE   RecName: Full=Purine nucleoside phosphorylase DeoD-type {ECO:0000255|HAMAP-Rule:MF_01627};
DE            Short=PNP {ECO:0000255|HAMAP-Rule:MF_01627};
DE            EC=2.4.2.1 {ECO:0000255|HAMAP-Rule:MF_01627};
DE   Flags: Fragment;
GN   Name=deoD {ECO:0000255|HAMAP-Rule:MF_01627};
OS   Streptococcus thermophilus.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Sfi6;
RX   PubMed=8626297; DOI=10.1128/jb.178.6.1680-1690.1996;
RA   Stingele F., Neeser J.R., Mollet B.;
RT   "Identification and characterization of the eps (Exopolysaccharide) gene
RT   cluster from Streptococcus thermophilus Sfi6.";
RL   J. Bacteriol. 178:1680-1690(1996).
CC   -!- FUNCTION: Catalyzes the reversible phosphorolytic breakdown of the N-
CC       glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the
CC       formation of the corresponding free purine bases and pentose-1-
CC       phosphate. {ECO:0000255|HAMAP-Rule:MF_01627}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a purine D-ribonucleoside + phosphate = a purine nucleobase +
CC         alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:19805, ChEBI:CHEBI:26386,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57720, ChEBI:CHEBI:142355; EC=2.4.2.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01627};
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:0000255|HAMAP-Rule:MF_01627};
CC   -!- SUBUNIT: Homohexamer; trimer of homodimers. {ECO:0000255|HAMAP-
CC       Rule:MF_01627}.
CC   -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01627, ECO:0000305}.
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DR   EMBL; U40830; AAC44007.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q56037; -.
DR   SMR; Q56037; -.
DR   eggNOG; COG0813; Bacteria.
DR   GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009164; P:nucleoside catabolic process; IEA:UniProt.
DR   CDD; cd09006; PNP_EcPNPI-like; 1.
DR   Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1.
DR   InterPro; IPR004402; DeoD-type.
DR   InterPro; IPR018016; Nucleoside_phosphorylase_CS.
DR   InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR   InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR   NCBIfam; TIGR00107; deoD; 1.
DR   PANTHER; PTHR43691:SF11; FI09636P-RELATED; 1.
DR   PANTHER; PTHR43691; URIDINE PHOSPHORYLASE; 1.
DR   Pfam; PF01048; PNP_UDP_1; 1.
DR   SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
DR   PROSITE; PS01232; PNP_UDP_1; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           <1..216
FT                   /note="Purine nucleoside phosphorylase DeoD-type"
FT                   /id="PRO_0000063166"
FT   ACT_SITE        184
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01627"
FT   BINDING         4
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:0000250|UniProtKB:P50389"
FT   BINDING         23
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P50389"
FT   BINDING         67..70
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:0000250|UniProtKB:P50389"
FT   BINDING         159..161
FT                   /ligand="a purine D-ribonucleoside"
FT                   /ligand_id="ChEBI:CHEBI:142355"
FT                   /evidence="ECO:0000250|UniProtKB:P50389"
FT   BINDING         183..184
FT                   /ligand="a purine D-ribonucleoside"
FT                   /ligand_id="ChEBI:CHEBI:142355"
FT                   /evidence="ECO:0000250|UniProtKB:P50389"
FT   SITE            198
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01627"
FT   NON_TER         1
SQ   SEQUENCE   216 AA;  24095 MW;  1BBC374D174CD5B3 CRC64;
     DPLRAKFIAE NFLEDAVCFN EVRNMFGYTG TYKGERISVM GTGMGMPSIS IYARELIVDY
     GVKKLIRVGT AGSLNENVHV RELVLAQAAA TNSNIIRNDW PQYDFPQIAS FNLLDKAYHI
     AKNFGMTTHV GNVLSSDEKY SNYFEKNIEL GKWGVKAVEM EAAALYYLAA QHQVDALAIM
     TISDSLVNPD EDTTAEERQN TFTDMMKVGL ETLIAD
//