ID   PSUG_MYXXD              Reviewed;         303 AA.
AC   Q1D739;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=MXAN_3335;
OS   Myxococcus xanthus (strain DK1622).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK1622;
RX   PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA   Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., Eisen J.,
RA   Ronning C.M., Barbazuk W.B., Blanchard M., Field C., Halling C., Hinkle G.,
RA   Iartchuk O., Kim H.S., Mackenzie C., Madupu R., Miller N., Shvartsbeyn A.,
RA   Sullivan S.A., Vaudin M., Wiegand R., Kaplan H.B.;
RT   "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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; CP000113; ABF92641.1; -; Genomic_DNA.
DR   RefSeq; WP_011553370.1; NC_008095.1.
DR   AlphaFoldDB; Q1D739; -.
DR   SMR; Q1D739; -.
DR   STRING; 246197.MXAN_3335; -.
DR   EnsemblBacteria; ABF92641; ABF92641; MXAN_3335.
DR   GeneID; 41360688; -.
DR   KEGG; mxa:MXAN_3335; -.
DR   eggNOG; COG2313; Bacteria.
DR   HOGENOM; CLU_012201_0_1_7; -.
DR   OMA; RKLGHRD; -.
DR   OrthoDB; 1294333at2; -.
DR   Proteomes; UP000002402; 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..303
FT                   /note="Pseudouridine-5'-phosphate glycosidase"
FT                   /id="PRO_0000390531"
FT   ACT_SITE        23
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   ACT_SITE        158
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   BINDING         85
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   BINDING         105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   BINDING         137
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   BINDING         139..141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
SQ   SEQUENCE   303 AA;  31787 MW;  B185DAD72985DD85 CRC64;
     MDLRFSEEVR RALEAGQPLV ALETSVVAQG LPYPDNLAAA RACEEAIRRA GAVPAATAII
     DGQLCVGLEE PEMRRLAEGK ERLLKVASRD FAVAMATRAT GGTTVSATCE MAAAAGIRVF
     STGGIGGVHR GASEHFDISQ DIAALARFPV AVVCAGAKSV LDLPKTMELL ETAGVPVIGV
     GTDELPSFYS RGSGIPLEHR ADDVDTAARI ARARFESLKQ GGVLYTVPPP EETSLPRNEV
     ELHIAATLAD ADRQGIRGKA VTPFLLSEMA KRTGGKTLKA NLALLTNNAR FAGQLAVAYA
     RAS