ID   PSUG_PARDP              Reviewed;         304 AA.
AC   A1B316;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=Pden_1813;
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA   Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL   Submitted (DEC-2006) 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; CP000489; ABL69910.1; -; Genomic_DNA.
DR   RefSeq; WP_011748107.1; NC_008686.1.
DR   AlphaFoldDB; A1B316; -.
DR   SMR; A1B316; -.
DR   STRING; 318586.Pden_1813; -.
DR   PRIDE; A1B316; -.
DR   EnsemblBacteria; ABL69910; ABL69910; Pden_1813.
DR   KEGG; pde:Pden_1813; -.
DR   eggNOG; COG2313; Bacteria.
DR   HOGENOM; CLU_012201_0_1_5; -.
DR   OMA; RKLGHRD; -.
DR   Proteomes; UP000000361; Chromosome 1.
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..304
FT                   /note="Pseudouridine-5'-phosphate glycosidase"
FT                   /id="PRO_0000390533"
FT   ACT_SITE        25
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   ACT_SITE        161
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   BINDING         108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   BINDING         140
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   BINDING         142..144
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
SQ   SEQUENCE   304 AA;  31517 MW;  CCAC168A6A36960C CRC64;
     MPPLIALSPE TSQALADRQP LVALESTIIT HGMPYPQNLE VAQQVEAAVR EEGAVPATIA
     VMGGRIRVGL DAEALEALAS TPAEQVMKLS RADLAACLAL GRTGATTVAA TMICAHLAGI
     EVFATGGIGG VHRGAETSFD ISADLQELAQ SPVTVVAAGA KAILDLPKTL EVLETLGVPV
     IAFGQDQLPA FWSRESGLAA PLRMDDPAQI AASARLRREL GLSGGQLVVN PIPPEAEIPR
     AEMIPVVEQA LSEAEAQGIA AKAVTPFLLQ RIFELTQGRS LDANIALVLN NARLAARIAA
     AMAT