ACL_RS03980
  | Uniprot: A9NGD7
Description: pseudouridine-5'-phosphate glycosidase EC number: 4.2.1.70 Annotation score: 3 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: Uracil + D-ribose 5-phosphate = pseudouridine 5'-phosphate + H(2)O. {ECO:0000255|HAMAP-Rule:MF_01876}. Cofactor: COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_01876}; ; Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01876} Enzyme regulation: Function [CC]: FUNCTION: Catalyzes the reversible cleavage of pseudouridine 5'-phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway. {ECO:0000255|HAMAP-Rule:MF_01876}. Pathway: Active site: ACT_SITE 25 25 Proton donor. {ECO:0000255|HAMAP-Rule:MF_01876}.; ACT_SITE 159 159 Nucleophile. {ECO:0000255|HAMAP-Rule:MF_01876}. Binding site: BINDING 86 86 Substrate. {ECO:0000255|HAMAP-Rule:MF_01876}.; BINDING 106 106 Substrate; via amide nitrogen. {ECO:0000255|HAMAP-Rule:MF_01876}. Calcium binding: DNA binding: Metal binding: METAL 138 138 Manganese. {ECO:0000255|HAMAP-Rule:MF_01876}. Nucleotide binding: Site: Gene names (primary): psuG Gene names (synonym): indA Mass: 32,480 Subunit structure [CC]: SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_01876}. Gene ontology (GO): hydrolase activity, acting on glycosyl bonds [GO:0016798]; metal ion binding [GO:0046872]; pseudouridylate synthase activity [GO:0004730]; nucleobase catabolic process [GO:0046113] Gene ontology IDs: GO:0004730; GO:0016798; GO:0046113; GO:0046872 Chain: CHAIN 1 303 Pseudouridine-5'-phosphate glycosidase. /FTId=PRO_0000390506. Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the pseudouridine-5'-phosphate glycosidase family. {ECO:0000255|HAMAP-Rule:MF_01876}. Protein families: Pseudouridine-5'-phosphate glycosidase family Coiled coil: Domain [FT]: Motif: Region: REGION 140 142 Substrate binding. {ECO:0000255|HAMAP-Rule:MF_01876}. EMBL: CP000896 ProteinModelPortal: A9NGD7 MEROPS: EnsemblBacteria KO: ABX81417 UniPathway: K16329 CDD: Gene3D: HAMAP: InterPro: MF_01876 PANTHER: IPR007342 PIRSF: PRINTS: PROSITE: Pfam: ProDom: PF04227 SMART: SUPFAM: TIGRFAMs: |
838412-839324(+) >nucleotide sequence GTTGTTGCGTTAGAATCTACGATTATTGCACATGGTATGCCTTATCCTAAAAATGTAGAA ACGGCACTCAATGTTGAAAAAATAGTTGAACAAAATGGTGCTATACCTGCGACAATTGCG ATTATAGATGGTCGTATTAAAGTGGGCTTAAATCCAAATGAACTTACATCGTTAGGAAAA CTTTCTAATGTACTCAAAGTATCCAAACGCGATATACCTTATTGTGTTATTAAAAAATAC AGTGGTGCTACTACCGTTTCAGCCACCATCCTTATTGCTGATATGGTAGGTATCAAAGTA TTTGCAACAGGTGGTATCGGTGGTGTACATAAGGATGCTGCTGCTACATTTGATATTTCA AGAGATCTTGAAGAAATTTCTGAAAAACAGGTCGCAGTTGTCTCAGCTGGGGCTAAAGCC ATACTAGACTTAGATCTTACACTAGAATATCTTGAGACCAAGGGTGTTGAAGTAATCGGA TATAAAACAAGTGAATTTCCTGCATTCTTTTCAAATGCATCTGGTTTAAATACTACTTTT CAATTAGATGAGGCAAGTCAAATTGCACAACTCATGTATACAAAATGGAATATGGGTTTA AGTGGTGGTATCGTCGTTGCAAATCCAATACCTCAAAATTACGCAATAGATAAAGACAGT TTAGATAAAGCAATTTCAAGTGCTATATTATCAGCTAAAGATAATAAAATTACTGGTAAA GAATTAACACCATACTTGCTTAAAATGCTACATAGTAACAAGGATATAACAAGTCTTGAA TCTAATATTGGTCTTATCTACAATAATGCGAAAATTGCAGCATTGATTGCTGTTGAATTT TCTAAACTTTAG >protein sequence IIDGRIKVGLNPNELTSLGKLSNVLKVSKRDIPYCVIKKYSGATTVSATILIADMVGIKV FATGGIGGVHKDAAATFDISRDLEEISEKQVAVVSAGAKAILDLDLTLEYLETKGVEVIG YKTSEFPAFFSNASGLNTTFQLDEASQIAQLMYTKWNMGLSGGIVVANPIPQNYAIDKDS LDKAISSAILSAKDNKITGKELTPYLLKMLHSNKDITSLESNIGLIYNNAKIAALIAVEF SKL |
© Fisunov Lab of Proteomics, 2016.