ID   PSUG1_PHOLL             Reviewed;         318 AA.
AC   Q7N4X5;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Pseudouridine-5'-phosphate glycosidase 1 {ECO:0000255|HAMAP-Rule:MF_01876};
DE            Short=PsiMP glycosidase 1 {ECO:0000255|HAMAP-Rule:MF_01876};
DE            EC=4.2.1.70 {ECO:0000255|HAMAP-Rule:MF_01876};
GN   Name=psuG1 {ECO:0000255|HAMAP-Rule:MF_01876}; OrderedLocusNames=plu2187;
OS   Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS   TT01).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=243265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15139 / CIP 105565 / TT01;
RX   PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA   Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA   Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(2003).
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; BX571866; CAE14480.1; -; Genomic_DNA.
DR   RefSeq; WP_011146441.1; NC_005126.1.
DR   AlphaFoldDB; Q7N4X5; -.
DR   SMR; Q7N4X5; -.
DR   STRING; 243265.plu2187; -.
DR   EnsemblBacteria; CAE14480; CAE14480; plu2187.
DR   GeneID; 24166451; -.
DR   KEGG; plu:plu2187; -.
DR   eggNOG; COG2313; Bacteria.
DR   HOGENOM; CLU_012201_0_1_6; -.
DR   OMA; PAFYCRS; -.
DR   OrthoDB; 1294333at2; -.
DR   BioCyc; PLUM243265:PLU_RS10925-MON; -.
DR   Proteomes; UP000002514; 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..318
FT                   /note="Pseudouridine-5'-phosphate glycosidase 1"
FT                   /id="PRO_0000390535"
FT   ACT_SITE        29
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   ACT_SITE        163
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   BINDING         90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   BINDING         110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   BINDING         142
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   BINDING         144..146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
SQ   SEQUENCE   318 AA;  33907 MW;  C372B44717CD44CE CRC64;
     MNISNKVPFK FSLEVKEALE SGKPVVALES NVITHGLDYP DNVTTAKNVE QAVRESGAIP
     ATIGIDKGEF LIGMSDEQIE KFATASHVPK VTSRDIPVVL ASGGMGATTV ASSILAAEIA
     GIKFFCSAGI GGVHRGAETS MDISADLTQL TRSRVAVVCA GAKNILDIGL TLEFLETWNV
     PVISYQSDDF PAFYCRSSGF KSPQRLDELA VIAKAIEINW MLPGGKGVLI TTPTKPEDAL
     DNQKIDIIIQ EAVLEAKKKN IVGNSLTKYL MRMVDRETDG ISAKANMAVL VNTAEVAGKL
     AVAACLQSST FFARIKSQ