O-acetyl-ADP-ribose deacetylase

Details

Name
O-acetyl-ADP-ribose deacetylase
Synonyms
  • 3.5.1.-
  • Regulator of RNase III activity
Gene Name
ymdB
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0019383|O-acetyl-ADP-ribose deacetylase
MKTRIHVVQGDITKLAVDVIVNAANPSLMGGGGVDGAIHRAAGPALLDACLKVRQQQGDC
PTGHAVITLAGDLPAKAVVHTVGPVWRGGEQNEDQLLQDAYLNSLRLVAANSYTSVAFPA
ISTGVYGYPRAAAAEIAVKTVSEFITRHALPEQVYFVCYDEENAHLYERLLTQQGDE
Number of residues
177
Molecular Weight
18880.25
Theoretical pI
5.52
GO Classification
Functions
enzyme binding / O-acetyl-ADP-ribose deacetylase activity / purine nucleoside binding / ribonuclease inhibitor activity
Processes
negative regulation of nuclease activity / negative regulation of ribonuclease activity / purine nucleoside metabolic process / regulation of single-species biofilm formation on inanimate substrate
General Function
Ribonuclease inhibitor activity
Specific Function
Deacetylates O-acetyl-ADP ribose. Down-regulates ribonuclease 3 (RNase III) activity. Acts by interacting directly with the region of the ribonuclease that is required for dimerization/activation.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0019384|O-acetyl-ADP-ribose deacetylase (ymdB)
ATGAAAACGCGTATTCATGTTGTGCAGGGTGATATTACCAAACTGGCCGTTGATGTGATT
GTGAATGCGGCTAATCCGTCATTAATGGGAGGCGGCGGCGTCGATGGGGCCATTCATCGC
GCAGCGGGTCCGGCCCTGCTGGATGCTTGTTTAAAAGTCAGGCAACAGCAGGGCGATTGC
CCTACGGGGCATGCCGTTATTACGCTTGCAGGCGATCTTCCCGCTAAAGCCGTAGTGCAC
ACCGTCGGGCCAGTCTGGCGTGGTGGTGAACAAAACGAAGACCAGCTTTTGCAGGATGCC
TATCTCAATAGCCTACGACTGGTGGCGGCAAACAGCTATACGTCAGTGGCTTTTCCTGCA
ATCAGTACTGGGGTTTATGGTTACCCTCGTGCGGCAGCGGCTGAAATCGCAGTAAAAACC
GTTTCAGAATTTATTACCCGTCACGCTTTACCCGAACAGGTATACTTTGTCTGTTATGAT
GAAGAAAACGCCCACCTCTACGAAAGACTCCTTACCCAACAAGGAGATGAATGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0A8D6
UniProtKB Entry NameYMDB_ECOLI
GenBank Gene IDU00096
General References
  1. Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. [Article]
  2. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  3. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  4. Kim KS, Manasherob R, Cohen SN: YmdB: a stress-responsive ribonuclease-binding regulator of E. coli RNase III activity. Genes Dev. 2008 Dec 15;22(24):3497-508. doi: 10.1101/gad.1729508. [Article]
  5. Chen D, Vollmar M, Rossi MN, Phillips C, Kraehenbuehl R, Slade D, Mehrotra PV, von Delft F, Crosthwaite SK, Gileadi O, Denu JM, Ahel I: Identification of macrodomain proteins as novel O-acetyl-ADP-ribose deacetylases. J Biol Chem. 2011 Apr 15;286(15):13261-71. doi: 10.1074/jbc.M110.206771. Epub 2011 Jan 21. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB038142-(N-morpholino)ethanesulfonic acidexperimentalunknownDetails