PSUG_LYSSC
ID PSUG_LYSSC Reviewed; 304 AA.
AC B1HV79;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, 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=Bsph_3909;
OS Lysinibacillus sphaericus (strain C3-41).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=444177;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C3-41;
RX PubMed=18296527; DOI=10.1128/jb.01652-07;
RA Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M.,
RA Berry C., Yuan Z.;
RT "Complete genome sequence of the mosquitocidal bacterium Bacillus
RT sphaericus C3-41 and comparison with those of closely related Bacillus
RT species.";
RL J. Bacteriol. 190:2892-2902(2008).
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; CP000817; ACA41381.1; -; Genomic_DNA.
DR RefSeq; WP_012295426.1; NC_010382.1.
DR AlphaFoldDB; B1HV79; -.
DR SMR; B1HV79; -.
DR EnsemblBacteria; ACA41381; ACA41381; Bsph_3909.
DR KEGG; lsp:Bsph_3909; -.
DR HOGENOM; CLU_012201_0_1_9; -.
DR OMA; RKLGHRD; -.
DR Proteomes; UP000002164; 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..304
FT /note="Pseudouridine-5'-phosphate glycosidase"
FT /id="PRO_0000390528"
FT ACT_SITE 25
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT ACT_SITE 159
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT BINDING 138
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT BINDING 140..142
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
SQ SEQUENCE 304 AA; 32139 MW; 28707286BADAFEFE CRC64;
MKEFIVLSEE VKAGQAKGLP IVALESTIIS HGMPYPQNVQ TAREVEQIIR DNGAVPATIA
LIDGKIKIGL SDEELEMFGN AQGVAKASRR DLGYLLATKK LGATTVAATM ICAELAGIEI
FVTGGIGGVH RGAETTMDVS ADLEELAQTN VAVICAGAKS ILDIGLTLEY LETKGVPVVG
YGTDELPAFY TRQSGFDVNF QLDTPEEIAE MLSAKWQLGL KGGAVIANPI PEAEALEHGF
ITNIIEKALV EAEENGIQGK NVTPFLLGKV KELTEGKSLD ANIALVKNNA VVGAKIAVAF
NQLH
