(data stored in ACNUC7421 zone)

SWISSPROT: PSUG_RUBXD

ID   PSUG_RUBXD              Reviewed;         302 AA.
AC   Q1AYR4;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   11-DEC-2019, entry version 69.
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=Rxyl_0490;
OS   Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129).
OC   Bacteria; Actinobacteria; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC   Rubrobacter.
OX   NCBI_TaxID=266117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9941 / NBRC 16129;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S.,
RA   Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.;
RT   "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL   Submitted (JUN-2006) 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}.
DR   EMBL; CP000386; ABG03464.1; -; Genomic_DNA.
DR   RefSeq; WP_011563482.1; NC_008148.1.
DR   SMR; Q1AYR4; -.
DR   STRING; 266117.Rxyl_0490; -.
DR   EnsemblBacteria; ABG03464; ABG03464; Rxyl_0490.
DR   KEGG; rxy:Rxyl_0490; -.
DR   eggNOG; ENOG4105D53; Bacteria.
DR   eggNOG; COG2313; LUCA.
DR   HOGENOM; HOG000064311; -.
DR   KO; K16329; -.
DR   OMA; IIAHGMP; -.
DR   OrthoDB; 1294333at2; -.
DR   BioCyc; RXYL266117:G1G6P-497-MONOMER; -.
DR   Proteomes; UP000006637; 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;
DR   PRODOM; Q1AYR4.
DR   SWISS-2DPAGE; Q1AYR4.
KW   Glycosidase; Hydrolase; Lyase; Manganese; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..302
FT                   /note="Pseudouridine-5'-phosphate glycosidase"
FT                   /id="PRO_0000390544"
FT   REGION          138..140
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   ACT_SITE        24
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   ACT_SITE        157
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   METAL           136
FT                   /note="Manganese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   BINDING         84
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   BINDING         104
FT                   /note="Substrate; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
SQ   SEQUENCE   302 AA;  31302 MW;  F7BF09A932272F75 CRC64;
     MRPVQPAPEV AEALEGGRPV VALESTLISH GLPRPDNLRV ARALEEAVRR EGAVPATVGV
     VGGVARVGLG PEELELLASG EVPKLSARDL PAAAATGSSG ATTVAATAHL AALCGIKLFA
     TGGLGGVHRG ARESWDVSAD LAALSRAPVA VVCSGVKSIL DVPATLEQLE TLGVPVVGFR
     SRSFAGFYLT DSGCALDWSV EDEGEAAALI RALPGLGLGC GVVISNPLPP EEQLDPSLHE
     RALRSGLEEL ARRGISGKEV TPFLLEHFRE RTGGESLRAN ERLVVRNARL AARIARRLAA
     GR
//

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