Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

O-acetyl-ADP-ribose deacetylase

Gene

ymdB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.UniRule annotation2 Publications

Kineticsi

  1. KM=270 µM for O-acetyl-ADP-ribose1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei35Proton acceptorUniRule annotation1

    GO - Molecular functioni

    • endoribonuclease inhibitor activity Source: EcoCyc
    • enzyme binding Source: EcoCyc
    • O-acetyl-ADP-ribose deacetylase activity Source: EcoCyc

    GO - Biological processi

    • negative regulation of endoribonuclease activity Source: EcoCyc
    • regulation of single-species biofilm formation on inanimate substrate Source: EcoCyc

    Keywordsi

    Molecular functionHydrolase
    Biological processStress response

    Enzyme and pathway databases

    BioCyciEcoCyc:G6550-MONOMER
    MetaCyc:G6550-MONOMER

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    O-acetyl-ADP-ribose deacetylaseUniRule annotation (EC:3.5.1.-UniRule annotation)
    Alternative name(s):
    Regulator of RNase III activityUniRule annotation
    Gene namesi
    Name:ymdBUniRule annotation
    Ordered Locus Names:b1045, JW1032
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG13874 ymdB

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi124G → E: Abolishes enzyme activity. 1 Publication1

    Chemistry databases

    DrugBankiDB03814 2-(N-Morpholino)-Ethanesulfonic Acid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000891911 – 177O-acetyl-ADP-ribose deacetylaseAdd BLAST177

    Proteomic databases

    PaxDbiP0A8D6
    PRIDEiP0A8D6

    Expressioni

    Inductioni

    Expression is induced by both entry into stationary phase, via RpoS, and cold-shock stress.1 Publication

    Interactioni

    Subunit structurei

    Homodimer. Interaction with the ribonuclease decreases homodimer formation.UniRule annotation1 Publication

    GO - Molecular functioni

    • enzyme binding Source: EcoCyc

    Protein-protein interaction databases

    BioGridi4260690, 29 interactors
    DIPiDIP-48222N
    IntActiP0A8D6, 3 interactors
    STRINGi316385.ECDH10B_1117

    Structurei

    Secondary structure

    1177
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 10Combined sources6
    Helixi12 – 14Combined sources3
    Beta strandi18 – 23Combined sources6
    Helixi34 – 42Combined sources9
    Helixi44 – 57Combined sources14
    Beta strandi65 – 69Combined sources5
    Beta strandi73 – 81Combined sources9
    Beta strandi87 – 92Combined sources6
    Helixi93 – 110Combined sources18
    Beta strandi115 – 118Combined sources4
    Helixi130 – 147Combined sources18
    Beta strandi149 – 160Combined sources12
    Helixi161 – 171Combined sources11

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1SPVX-ray2.00A1-176[»]
    5CB3X-ray1.80A1-177[»]
    5CB5X-ray2.80A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R1-177[»]
    5CMSX-ray2.98A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R1-177[»]
    ProteinModelPortaliP0A8D6
    SMRiP0A8D6
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A8D6

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini1 – 175MacroUniRule annotationAdd BLAST175

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni121 – 127Substrate bindingCurated7

    Sequence similaritiesi

    Belongs to the YmdB family.Curated

    Phylogenomic databases

    eggNOGiENOG4108UVJ Bacteria
    COG2110 LUCA
    HOGENOMiHOG000086960
    InParanoidiP0A8D6
    OMAiLASCYRE
    PhylomeDBiP0A8D6

    Family and domain databases

    HAMAPiMF_01205 YmdB, 1 hit
    InterProiView protein in InterPro
    IPR002589 Macro_dom
    IPR024900 O-Ac-ADP-ribose_deAcase
    PfamiView protein in Pfam
    PF01661 Macro, 1 hit
    SMARTiView protein in SMART
    SM00506 A1pp, 1 hit
    PROSITEiView protein in PROSITE
    PS51154 MACRO, 1 hit

    Sequencei

    Sequence statusi: Complete.

    P0A8D6-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKTRIHVVQG DITKLAVDVI VNAANPSLMG GGGVDGAIHR AAGPALLDAC
    60 70 80 90 100
    LKVRQQQGDC PTGHAVITLA GDLPAKAVVH TVGPVWRGGE QNEDQLLQDA
    110 120 130 140 150
    YLNSLRLVAA NSYTSVAFPA ISTGVYGYPR AAAAEIAVKT VSEFITRHAL
    160 170
    PEQVYFVCYD EENAHLYERL LTQQGDE
    Length:177
    Mass (Da):18,880
    Last modified:June 7, 2005 - v1
    Checksum:i6F4E12D5C181CAAF
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA Translation: AAC74129.1
    AP009048 Genomic DNA Translation: BAA35835.1
    PIRiB64847
    RefSeqiNP_415563.1, NC_000913.3
    WP_000857405.1, NZ_LN832404.1

    Genome annotation databases

    EnsemblBacteriaiAAC74129; AAC74129; b1045
    BAA35835; BAA35835; BAA35835
    GeneIDi946987
    KEGGiecj:JW1032
    eco:b1045
    PATRICifig|1411691.4.peg.1224

    Similar proteinsi

    Entry informationi

    Entry nameiYMDB_ECOLI
    AccessioniPrimary (citable) accession number: P0A8D6
    Secondary accession number(s): P75918
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: June 7, 2005
    Last modified: March 28, 2018
    This is version 95 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Cookie policy

    We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health