AC   MF_01627;
DC   Protein; auto
TR   HAMAP; MF_01627; -; 1; level=0
XX
Names: Pur_nucleosid_phosp
XX
ID   DEOD
DE   RecName: Full=Purine nucleoside phosphorylase DeoD-type;
DE            Short=PNP;
DE            EC=2.4.2.1;
GN   Name=deoD;
XX
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.
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   -!- 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   -!- SUBUNIT: Homohexamer; trimer of homodimers.
CC   -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family.
XX
DR   PROSITE; PS01232; PNP_UDP_1; 1; trigger=no
DR   Pfam; PF01048; PNP_UDP_1; 1; trigger=no
DR   NCBIfam; TIGR00107; deoD; 1; trigger=no
XX
case <FTTag:acetylation>
KW   Acetylation
end case
KW   Glycosyltransferase
KW   Transferase
XX
GO   GO:0004731; F:purine-nucleoside phosphorylase activity
GO   GO:0042278; P:purine nucleoside metabolic process
XX
FT   From: DEOD_ECOLI (P0ABP8)
FT   ACT_SITE        205
FT                   /note="Proton donor"
FT   Condition: D
FT   SITE            218
FT                   /note="Important for catalytic activity"
FT   Condition: R
FT   BINDING         88..91
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT   Condition: R-[IV]-G-[TS]
FT   BINDING         180..182
FT                   /ligand="a purine D-ribonucleoside"
FT                   /ligand_id="ChEBI:CHEBI:142355"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT   Condition: [ED]-M-E
FT   BINDING         204..205
FT                   /ligand="a purine D-ribonucleoside"
FT                   /ligand_id="ChEBI:CHEBI:142355"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT   Condition: [ST]-[DN]
FT   BINDING         5
FT                   /ligand="a purine D-ribonucleoside"
FT                   /ligand_id="ChEBI:CHEBI:142355"
FT                   /ligand_note="ligand shared between dimeric partners"
FT   Condition: H
FT   BINDING         21
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT   Condition: G
FT   BINDING         25
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT   Condition: R
FT   BINDING         44
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /ligand_note="ligand shared between dimeric partners"
FT   Condition: R
case <OC:Escherichia> or <OC:Shigella>
FT   MOD_RES         27
FT                   /note="N6-acetyllysine"
FT   Tag: acetylation; Condition: K
end case
XX
Size: 220-270;
Related: None;
Template: P0ABP8; Q8ZJV7;
Scope:
 Bacteria; Bacillota
 Bacteria; Pseudomonadota
Fusion:
 Nter: None
 Cter: None
Duplicate: in PHOPR, SHEON, VIBCH, ALIF1, VIBPA, VIBVU, VIBVY
Plasmid: None
Comments: None
XX
# Revision 1.25 2023/06/01
//