ID   PSUG_PSELT              Reviewed;         284 AA.
AC   A8F8N4;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
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}; OrderedLocusNames=Tlet_1964;
OS   Pseudothermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / NBRC 107922 /
OS   TMO) (Thermotoga lettingae).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Pseudothermotoga.
OX   NCBI_TaxID=416591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Foster B., Bruce D., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA   Richardson P.;
RT   "Complete sequence of Thermotoga lettingae TMO.";
RL   Submitted (AUG-2007) 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; CP000812; ABV34518.1; -; Genomic_DNA.
DR   RefSeq; WP_012003994.1; NC_009828.1.
DR   AlphaFoldDB; A8F8N4; -.
DR   SMR; A8F8N4; -.
DR   STRING; 416591.Tlet_1964; -.
DR   EnsemblBacteria; ABV34518; ABV34518; Tlet_1964.
DR   KEGG; tle:Tlet_1964; -.
DR   eggNOG; COG2313; Bacteria.
DR   HOGENOM; CLU_012201_0_1_0; -.
DR   OMA; RKLGHRD; -.
DR   OrthoDB; 1294333at2; -.
DR   Proteomes; UP000002016; 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..284
FT                   /note="Pseudouridine-5'-phosphate glycosidase"
FT                   /id="PRO_0000390554"
FT   ACT_SITE        8
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   ACT_SITE        140
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   BINDING         69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   BINDING         89
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   BINDING         119
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   BINDING         121..123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
SQ   SEQUENCE   284 AA;  31324 MW;  B71247C8E1ABEFA2 CRC64;
     MEKILALEST VIAHGLPFPI NIDTAVELEE LAAETGCSAK TIGIIAGQIK VGLSREEIVQ
     IASRKDVLKI GTAEIPFALA KKMWAATTVS ATMRIAHLNN IKVFATGGIG GVHKIDQWDV
     SQDLAELSRT RMIVVSAGPK SILDLRSTVE MLETFQITVV GYKTDELPAF YCKSTSIHIN
     RVDSFEEIAS IFLFKEKFNL PGAVLVFNPI PDEHAIEVEQ FEEWYRLSEH DLDASSVKGK
     GVTPFLLSRL AHYSKGKTVR SNVELLKNNV KVACEILNQL SKMQ