AC   MF_01876;
DC   Protein; auto
TR   HAMAP; MF_01876; -; 1; level=0
XX
Names: PsiMP_glycosidase
XX
ID   PSUG
DE   RecName: Full=Pseudouridine-5'-phosphate glycosidase;
DE            Short=PsiMP glycosidase;
DE            EC=4.2.1.70;
GN   Name=psuG;
XX
CC   -!- FUNCTION: Catalyzes the reversible cleavage of pseudouridine 5'-
CC       phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions
CC       biologically in the cleavage direction, as part of a pseudouridine
CC       degradation pathway.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-ribose 5-phosphate + uracil = H2O + psi-UMP;
CC         Xref=Rhea:RHEA:18337, ChEBI:CHEBI:15377, ChEBI:CHEBI:17568,
CC         ChEBI:CHEBI:58380, ChEBI:CHEBI:78346; EC=4.2.1.70;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC       Note=Binds 1 Mn(2+) ion per subunit.;
CC   -!- SUBUNIT: Homotrimer.
CC   -!- SIMILARITY: Belongs to the pseudouridine-5'-phosphate glycosidase
CC       family.
XX
DR   Pfam; PF04227; Indigoidine_A; 1; trigger=no
XX
KW   Glycosidase
KW   Hydrolase
KW   Lyase
KW   Manganese
KW   Metal-binding
XX
GO   GO:0004730; F:pseudouridylate synthase activity
GO   GO:0046113; P:nucleobase catabolic process
XX
FT   From: PSUG_ECOLI (P33025)
FT   BINDING         147..149
FT                   /ligand="substrate"
FT   Condition: S-x-D
FT   ACT_SITE        31
FT                   /note="Proton donor"
FT   Condition: E
FT   ACT_SITE        166
FT                   /note="Nucleophile"
FT   Condition: K
FT   BINDING         145
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   Condition: D
FT   BINDING         93
FT                   /ligand="substrate"
FT   Condition: K
FT   BINDING         113
FT                   /ligand="substrate"
FT   Condition: [VA]
XX
Size: 270-369;
Related: None;
Template: P33025; Q9X1H5;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: in ECO7I, PHOLL, RHIJ3
Plasmid: in PARP8, CORA7, RHIJ3
Comments: None
XX
# Revision 1.14 2023/11/28
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