PSUG_SALTO
ID PSUG_SALTO Reviewed; 324 AA.
AC A4X4Y7;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=Strop_1471;
OS Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440).
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Salinispora.
OX NCBI_TaxID=369723;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440;
RX PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA Jensen P.R., Moore B.S.;
RT "Genome sequencing reveals complex secondary metabolome in the marine
RT actinomycete Salinispora tropica.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(2007).
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; CP000667; ABP53937.1; -; Genomic_DNA.
DR AlphaFoldDB; A4X4Y7; -.
DR SMR; A4X4Y7; -.
DR STRING; 369723.Strop_1471; -.
DR EnsemblBacteria; ABP53937; ABP53937; Strop_1471.
DR KEGG; stp:Strop_1471; -.
DR eggNOG; COG2313; Bacteria.
DR HOGENOM; CLU_012201_0_1_11; -.
DR OMA; RKLGHRD; -.
DR Proteomes; UP000000235; 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..324
FT /note="Pseudouridine-5'-phosphate glycosidase"
FT /id="PRO_0000390546"
FT ACT_SITE 43
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT ACT_SITE 177
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT BINDING 156
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT BINDING 158..160
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
SQ SEQUENCE 324 AA; 33625 MW; C8309504DCA9D157 CRC64;
MPGLLRARRT DAVRLDAVTT FHLRHGVEVA DALRVGRPVV ALESTIVSHG LPRPDNLRVA
REIEQTVRDA GAVPATIGMV AGQLVVGLDD AELTRLATVD DVAKLSVRDL AVAAATDADG
ATTVAATSAV AAAAGIRVFA TGGLGGVHRE AAQSFDESAD LTTLARTPIA VVCAGVKSIL
DSGATLERLE TLGVGVVGYR TRRFPGFYLT DGGFDLDWSV DSPEQVAAAL AAQEQHGLHS
GGLVVANPLP TDEQLDPALH DRTLAEGLML LRREGVTGKA VTPFLLAHFH SATEGASLAV
NIRIILRNAD LAAQIAVASA ARQA
