(data stored in ACNUC7421 zone)

SWISSPROT: PSUG_RHILO

ID   PSUG_RHILO              Reviewed;         305 AA.
AC   Q98NQ8;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   11-DEC-2019, entry version 87.
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=mll0028;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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; BA000012; BAB47703.1; -; Genomic_DNA.
DR   RefSeq; WP_010909073.1; NC_002678.2.
DR   SMR; Q98NQ8; -.
DR   STRING; 266835.14021090; -.
DR   EnsemblBacteria; BAB47703; BAB47703; BAB47703.
DR   KEGG; mlo:mll0028; -.
DR   PATRIC; fig|266835.9.peg.23; -.
DR   eggNOG; ENOG4105D53; Bacteria.
DR   eggNOG; COG2313; LUCA.
DR   HOGENOM; HOG000064311; -.
DR   KO; K16329; -.
DR   OMA; IIAHGMP; -.
DR   OrthoDB; 1294333at2; -.
DR   BioCyc; MLOT266835:G1G20-22-MONOMER; -.
DR   Proteomes; UP000000552; 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; Q98NQ8.
DR   SWISS-2DPAGE; Q98NQ8.
KW   Glycosidase; Hydrolase; Lyase; Manganese; Metal-binding.
FT   CHAIN           1..305
FT                   /note="Pseudouridine-5'-phosphate glycosidase"
FT                   /id="PRO_0000390540"
FT   REGION          145..147
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   ACT_SITE        30
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   ACT_SITE        164
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   METAL           143
FT                   /note="Manganese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   BINDING         91
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
FT   BINDING         111
FT                   /note="Substrate; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01876"
SQ   SEQUENCE   305 AA;  31575 MW;  8080DA15EA570ADB CRC64;
     MSPETARPFI DIHAPVAQAL AAGRPVVALE STIITHGMPY PDNGAMAANV EKIISDGGAV
     PATIAVIGGR IKIGLSDGER ESLAMTGDAM KLSRADLGFA VAQGRTGGTT VAATMIAAEM
     VGIKVFATGG IGGVHKGAEK SFDISADLDE LARTPVIVVS AGAKAILDIE KTLEVLETRG
     VPVVGHGCET MPAFWSRQSP FRAPLTLYKP EEIAHFFRTR VALGLGGGVL VANPVPENHE
     IPAEEMAGYI EAAQKAAEAL NVTGKAVTPF LLGKILELTG GRSLKTNIAL VENNARLAAE
     IAKAL
//

If you have problems or comments...

PBIL Back to PBIL home page