PSUG_CLOBL
ID PSUG_CLOBL Reviewed; 307 AA.
AC A7GCK7;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=CLI_1251;
OS Clostridium botulinum (strain Langeland / NCTC 10281 / Type F).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441772;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Langeland / NCTC 10281 / Type F;
RA Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., Bruce D.,
RA Detter C., Munk C., Smith L.A., Smith T.J., White O., Brettin T.S.;
RL Submitted (JUN-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; CP000728; ABS42209.1; -; Genomic_DNA.
DR RefSeq; WP_003487170.1; NC_009699.1.
DR AlphaFoldDB; A7GCK7; -.
DR SMR; A7GCK7; -.
DR EnsemblBacteria; ABS42209; ABS42209; CLI_1251.
DR KEGG; cbf:CLI_1251; -.
DR HOGENOM; CLU_012201_0_1_9; -.
DR OMA; RKLGHRD; -.
DR Proteomes; UP000002410; 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.
FT CHAIN 1..307
FT /note="Pseudouridine-5'-phosphate glycosidase"
FT /id="PRO_0000390512"
FT ACT_SITE 26
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 307 AA; 33039 MW; C2A9E32E6793BFF8 CRC64;
MLEKYLEISK EVSEALKENK PVVALESTII SHGMPYPKNA ETALNVEKII RDKGAIPATI
AILNGKLKVG LTKDEIEYLG KKGKEVVKTS RRDIPFILAK KLDGATTVAS TMIVANLAGI
KVFGTGGIGG VHRGAQESFD ISADLQELAN TNVAVVCAGA KSILDIGLTL EYLETQGVPV
VGFGTEELPA FYTRKSGFKV DYRVDTAKEL AEALKAKWDL GLKGGMVVGN PIPEEYQMDY
DTITKAINDA VKEAEEKGIK GKESTPFLLA KVKDITKGKS LEANIQLVYN NVAVASDLAI
ELSKLNK
