PSUG2_RHIL3
ID PSUG2_RHIL3 Reviewed; 309 AA.
AC Q1M4T3;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Pseudouridine-5'-phosphate glycosidase 2 {ECO:0000255|HAMAP-Rule:MF_01876};
DE Short=PsiMP glycosidase 2 {ECO:0000255|HAMAP-Rule:MF_01876};
DE EC=4.2.1.70 {ECO:0000255|HAMAP-Rule:MF_01876};
GN Name=psuG2 {ECO:0000255|HAMAP-Rule:MF_01876}; OrderedLocusNames=pRL120175;
OS Rhizobium leguminosarum bv. viciae (strain 3841).
OG Plasmid pRL12.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=216596;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3841;
RX PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT components.";
RL Genome Biol. 7:R34.1-R34.20(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; AM236086; CAK11888.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1M4T3; -.
DR SMR; Q1M4T3; -.
DR STRING; 216596.pRL120175; -.
DR EnsemblBacteria; CAK11888; CAK11888; pRL120175.
DR KEGG; rle:pRL120175; -.
DR eggNOG; COG2313; Bacteria.
DR HOGENOM; CLU_012201_0_1_5; -.
DR OMA; PAFYCRS; -.
DR Proteomes; UP000006575; Plasmid pRL12.
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; Plasmid.
FT CHAIN 1..309
FT /note="Pseudouridine-5'-phosphate glycosidase 2"
FT /id="PRO_0000390539"
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 309 AA; 32889 MW; ED110D59D1FF069E CRC64;
MTLMKPRLSR EMAEAIAAGS PVVALESTII THGMPYPANL ETALGVETVI RENGAIPATI
AVVKGELRVG LEHDELEELA QSKGIVKASG RDLAVAMIRG QSAGTTVSAT MLMADLAGID
VFATGGVGGV HRGAEQTFDI SADLTELGRT KTAVVCAGVK SILDIAKTLE YLETQRVPVI
AYGTEDFPAF FTRRSGFKAD HRLDTPEEIA KAMWLHHQLG TGTGLLIANP IPEASALAPD
FIDGTIADAV RDADERGIDR KELTPFLLAR INELTKGESL KANIELVKNN ARLAARIAVA
YAPLKKARN
