PSUG_LEGPH
ID PSUG_LEGPH Reviewed; 308 AA.
AC Q5ZU79;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
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}; Synonyms=indA;
GN OrderedLocusNames=lpg1928;
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE017354; AAU27998.1; -; Genomic_DNA.
DR RefSeq; WP_010947645.1; NC_002942.5.
DR RefSeq; YP_095945.1; NC_002942.5.
DR AlphaFoldDB; Q5ZU79; -.
DR SMR; Q5ZU79; -.
DR STRING; 272624.lpg1928; -.
DR PaxDb; Q5ZU79; -.
DR EnsemblBacteria; AAU27998; AAU27998; lpg1928.
DR GeneID; 66491060; -.
DR KEGG; lpn:lpg1928; -.
DR PATRIC; fig|272624.6.peg.2013; -.
DR eggNOG; COG2313; Bacteria.
DR HOGENOM; CLU_012201_0_1_6; -.
DR OMA; RKLGHRD; -.
DR Proteomes; UP000000609; 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..308
FT /note="Pseudouridine-5'-phosphate glycosidase"
FT /id="PRO_0000390527"
FT ACT_SITE 26
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT ACT_SITE 160
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT BINDING 139
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT BINDING 141..143
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
SQ SEQUENCE 308 AA; 33570 MW; 85A94E67D7433BEC CRC64;
MFHDLLEFNE EVLDAINDKN PIVALESTII SHGMPYPDNL TTAIEVENII RRQGAIPATI
AMHQGKIRVG LTQEVMEHLA LQKEVIKASR RDISFVLSRK VTASTTVAAT MFCAHMAKLP
LFVTGGIGGV HQDVTMSFDI SADLIELSNT PVTVVCSGAK SILDLPKTLE VLETFGVPVI
GYATDEFPAF YSRSSGIPVP QRLNSAEEVA NLMSIQQKLN MKNGIVVANP IPVSAELSDE
EISPYIKQAH DEAKHMSGKS LTPFLLKRIA ELTAGKSLEA NIELIKNNAF LGAEIAIAYQ
KKLFSKKT