ID   PSUG_COPPD              Reviewed;         302 AA.
AC   B5Y6G9;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Pseudouridine-5'-phosphate glycosidase {ECO:0000255|HAMAP-Rule:MF_01876};
DE            Short=PsiMP glycosidase {ECO:0000255|HAMAP-Rule:MF_01876};
DE            EC=4.2.1.70 {ECO:0000255|HAMAP-Rule:MF_01876};
GN   Name=psuG {ECO:0000255|HAMAP-Rule:MF_01876};
GN   OrderedLocusNames=COPRO5265_1592;
OS   Coprothermobacter proteolyticus (strain ATCC 35245 / DSM 5265 / OCM 4 /
OS   BT).
OC   Bacteria; Coprothermobacterota; Coprothermobacteria; Coprothermobacterales;
OC   Coprothermobacteraceae; Coprothermobacter.
OX   NCBI_TaxID=309798;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35245 / DSM 5265 / OCM 4 / BT;
RA   Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT   "The complete genome sequence of Coprothermobacter proteolyticus strain
RT   ATCC 5245 / DSM 5265 / BT.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-Rule:MF_01876}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_01876};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01876};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01876};
CC   -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_01876}.
CC   -!- SIMILARITY: Belongs to the pseudouridine-5'-phosphate glycosidase
CC       family. {ECO:0000255|HAMAP-Rule:MF_01876}.
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DR   EMBL; CP001145; ACI17404.1; -; Genomic_DNA.
DR   RefSeq; WP_012544056.1; NC_011295.1.
DR   AlphaFoldDB; B5Y6G9; -.
DR   SMR; B5Y6G9; -.
DR   STRING; 309798.COPRO5265_1592; -.
DR   EnsemblBacteria; ACI17404; ACI17404; COPRO5265_1592.
DR   KEGG; cpo:COPRO5265_1592; -.
DR   eggNOG; COG2313; Bacteria.
DR   HOGENOM; CLU_012201_0_1_9; -.
DR   OMA; RKLGHRD; -.
DR   OrthoDB; 1294333at2; -.
DR   Proteomes; UP000001732; Chromosome.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004730; F:pseudouridylate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046113; P:nucleobase catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.1790.10; -; 1.
DR   HAMAP; MF_01876; PsiMP_glycosidase; 1.
DR   InterPro; IPR022830; Indigdn_synthA-like.
DR   InterPro; IPR007342; PsuG.
DR   PANTHER; PTHR42909; PTHR42909; 1.
DR   Pfam; PF04227; Indigoidine_A; 1.
DR   SUPFAM; SSF110581; SSF110581; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; Lyase; Manganese; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..302
FT                   /note="Pseudouridine-5'-phosphate glycosidase"
FT                   /id="PRO_0000390513"
FT   ACT_SITE        22
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   ACT_SITE        156
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   BINDING         83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   BINDING         103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   BINDING         135
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   BINDING         137..139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
SQ   SEQUENCE   302 AA;  32113 MW;  87ED4276A0E39597 CRC64;
     MLQIAPHVKE AIETLKPVVA LESTIITHGM PYPANLHTAL EVEQVIKEAG AVPATIGVIN
     GIIKVGLSEE EITYLSQAKD LHKISLKDLS VAAAKKLSGG TTVSATMFAS YKAGIQVFAT
     GGIGGVHRDA RESFDVSTDL EALGSIPITV VCAGAKAILD LPATLEYLET KGVLVVGYKT
     DEFPAFYYGR SGLKLEHSVT TPGELAQIIR ERDALEINKA ILVGNPPPEE MALEKGKVEQ
     LIEAALQQAK VNNIKGKDVT PFLLDYLAKN SKGETLETNI ALVKNNAYVG SLIAKALMAA
     KI