Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P06134

- ADA_ECOLI

UniProt

P06134 - ADA_ECOLI

Protein

Bifunctional transcriptional activator/DNA repair enzyme Ada

Gene

ada

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 2 (01 Feb 1994)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Is involved in the adaptive response to alkylation damage in DNA caused by alkylating agents. Repairs O6-methylguanine and 04-methylthymine residues in alkylated DNA by a direct and irreversible transfer of the methyl group from the base to one of its own cysteine residues (Cys-321). Also specifically repairs the Sp diastereomer of DNA methylphosphotriester lesions by the same mechanism, although the methyl transfer occurs onto a different cysteine residue (Cys-38). Can not demethylate the other diastereomer, Rp-methylphosphotriester.1 Publication
    The methylation of Ada by methylphosphotriesters in DNA leads to its activation as a transcriptional regulator that activates the transcription of its own gene, ada, and other alkylation resistance genes, alkA, alkB and aidB.1 Publication

    Catalytic activityi

    DNA (containing Sp-methylphosphotriester) + protein L-cysteine = DNA (without Sp-methylphosphotriester) + protein S-methyl-L-cysteine.1 Publication
    DNA (containing 6-O-methylguanine) + protein L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L-cysteine.1 PublicationPROSITE-ProRule annotation

    Cofactori

    Binds 1 zinc ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei34 – 341DNA1 Publication
    Active sitei38 – 381Nucleophile; methyl group acceptor from methylphosphotriester2 PublicationsPROSITE-ProRule annotation
    Metal bindingi38 – 381Zinc
    Metal bindingi42 – 421Zinc
    Binding sitei43 – 431DNA1 Publication
    Binding sitei45 – 451DNA1 Publication
    Binding sitei67 – 671DNA1 Publication
    Metal bindingi69 – 691Zinc
    Metal bindingi72 – 721Zinc
    Sitei128 – 1292Cleavage
    Sitei178 – 1792Cleavage
    Active sitei321 – 3211Nucleophile; methyl group acceptor from either O6-methylguanine or O4-methylthymine1 PublicationPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi102 – 12120H-T-H motifPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. methylated-DNA-[protein]-cysteine S-methyltransferase activity Source: EcoliWiki
    2. protein binding Source: IntAct
    3. sequence-specific DNA binding Source: InterPro
    4. sequence-specific DNA binding transcription factor activity Source: InterPro
    5. zinc ion binding Source: EcoliWiki

    GO - Biological processi

    1. DNA dealkylation involved in DNA repair Source: EcoliWiki
    2. DNA demethylation Source: EcoliWiki
    3. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Methyltransferase, Transferase

    Keywords - Biological processi

    DNA damage, DNA repair, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:PD00230.
    ECOL316407:JW2201-MONOMER.
    MetaCyc:PD00230.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional transcriptional activator/DNA repair enzyme Ada
    Alternative name(s):
    Regulatory protein of adaptive response
    Including the following 2 domains:
    Methylphosphotriester-DNA--protein-cysteine S-methyltransferase (EC:2.1.1.n11)
    Alternative name(s):
    Methylphosphotriester-DNA methyltransferase
    Methylated-DNA--protein-cysteine methyltransferase (EC:2.1.1.63)
    Alternative name(s):
    O6-methylguanine-DNA alkyltransferase
    Gene namesi
    Name:ada
    Ordered Locus Names:b2213, JW2201
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10029. ada.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 354354Bifunctional transcriptional activator/DNA repair enzyme AdaPRO_0000018747Add
    BLAST

    Proteomic databases

    PRIDEiP06134.

    Expressioni

    Inductioni

    Up-regulated by methylated Ada itself in response to the exposure to alkylating agents.

    Gene expression databases

    GenevestigatoriP06134.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    hdaP699313EBI-1119501,EBI-545453

    Protein-protein interaction databases

    DIPiDIP-9055N.
    IntActiP06134. 13 interactions.
    MINTiMINT-1310041.
    STRINGi511145.b2213.

    Structurei

    Secondary structure

    1
    354
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 63
    Helixi9 – 179
    Helixi21 – 233
    Turni24 – 263
    Beta strandi27 – 315
    Turni32 – 343
    Beta strandi36 – 383
    Helixi49 – 513
    Beta strandi52 – 576
    Helixi58 – 636
    Beta strandi67 – 693
    Turni70 – 723
    Beta strandi76 – 783
    Helixi79 – 9315
    Beta strandi96 – 983
    Helixi102 – 1098
    Helixi113 – 12311
    Helixi128 – 13710
    Turni142 – 1443
    Beta strandi190 – 1967
    Beta strandi199 – 2057
    Beta strandi207 – 21711
    Helixi219 – 22911
    Helixi240 – 25415
    Beta strandi255 – 2573
    Helixi270 – 27910
    Helixi290 – 2967
    Helixi303 – 3119
    Helixi321 – 3233
    Helixi338 – 34811

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ADNNMR-A1-92[»]
    1EYFNMR-A1-92[»]
    1SFEX-ray2.10A175-354[»]
    1U8BX-ray2.10A9-139[»]
    1WPKNMR-A1-146[»]
    1ZGWNMR-A1-139[»]
    ProteinModelPortaliP06134.
    SMRiP06134. Positions 1-146, 187-351.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06134.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini85 – 18399HTH araC/xylS-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 171171Methylphosphotriester-DNA--protein-cysteine methyltransferaseAdd
    BLAST
    Regioni181 – 354174Methylated-DNA--protein-cysteine methyltransferaseAdd
    BLAST

    Domaini

    Consists of two domains. The 20 kDa N-terminal domain repairs the Sp diastereomer of methylphosphotriesters and, in its methylated form, binds DNA in a sequence-specific manner. The 19 kDa C-terminal domain repairs the mutagenic lesions O6-methylguanine. Each domain retains its activity when separated form the other.1 Publication

    Sequence similaritiesi

    In the C-terminal section; belongs to the MGMT family.Curated
    Contains 1 HTH araC/xylS-type DNA-binding domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG2169.
    HOGENOMiHOG000244139.
    KOiK10778.
    OMAiGMRPRQY.
    OrthoDBiEOG6WMJ4F.
    PhylomeDBiP06134.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    1.10.10.60. 1 hit.
    3.40.10.10. 1 hit.
    InterProiIPR004026. Ada_DNA_repair_Zn-bd.
    IPR016221. Bifunct_regulatory_prot_Ada.
    IPR009057. Homeodomain-like.
    IPR018060. HTH_AraC.
    IPR018062. HTH_AraC-typ_CS.
    IPR001497. MethylDNA_cys_MeTrfase_AS.
    IPR014048. MethylDNA_cys_MeTrfase_DNA-bd.
    IPR008332. MethylG_MeTrfase_N.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF02805. Ada_Zn_binding. 1 hit.
    PF01035. DNA_binding_1. 1 hit.
    PF00165. HTH_AraC. 2 hits.
    PF02870. Methyltransf_1N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000409. Ada. 1 hit.
    SMARTiSM00342. HTH_ARAC. 1 hit.
    [Graphical view]
    SUPFAMiSSF46689. SSF46689. 1 hit.
    SSF46767. SSF46767. 1 hit.
    SSF53155. SSF53155. 1 hit.
    SSF57884. SSF57884. 1 hit.
    TIGRFAMsiTIGR00589. ogt. 1 hit.
    PROSITEiPS00041. HTH_ARAC_FAMILY_1. 2 hits.
    PS01124. HTH_ARAC_FAMILY_2. 1 hit.
    PS00374. MGMT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P06134-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKATCLTDD QRWQSVLARD PNADGEFVFA VRTTGIFCRP SCRARHALRE    50
    NVSFYANASE ALAAGFRPCK RCQPEKANAQ QHRLDKITHA CRLLEQETPV 100
    TLEALADQVA MSPFHLHRLF KATTGMTPKA WQQAWRARRL RESLAKGESV 150
    TTSILNAGFP DSSSYYRKAD ETLGMTAKQF RHGGENLAVR YALADCELGR 200
    CLVAESERGI CAILLGDDDA TLISELQQMF PAADNAPADL MFQQHVREVI 250
    ASLNQRDTPL TLPLDIRGTA FQQQVWQALR TIPCGETVSY QQLANAIGKP 300
    KAVRAVASAC AANKLAIIIP CHRVVRGDGT LSGYRWGVSR KAQLLRREAE 350
    NEER 354
    Length:354
    Mass (Da):39,324
    Last modified:February 1, 1994 - v2
    Checksum:i4163E585C768C2F4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti134 – 1341A → R in AAA23412. (PubMed:2987251)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti75 – 751E → D in strain: B.
    Natural varianti79 – 802AQ → PR in strain: B.
    Natural varianti318 – 3181I → V in strain: B.
    Natural varianti330 – 3301T → S in strain: B.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M10211 Genomic DNA. Translation: AAA23412.1.
    M10315 Genomic DNA. Translation: AAA23413.1.
    U00008 Genomic DNA. Translation: AAA16408.1.
    U00096 Genomic DNA. Translation: AAC75273.1.
    AP009048 Genomic DNA. Translation: BAA15996.1.
    J02607 Genomic DNA. Translation: AAA23415.1.
    M13155 Genomic DNA. Translation: AAA23418.1.
    M13828 Genomic DNA. Translation: AAA23417.1.
    PIRiC64991. XYECO2.
    RefSeqiNP_416717.1. NC_000913.3.
    YP_490451.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75273; AAC75273; b2213.
    BAA15996; BAA15996; BAA15996.
    GeneIDi12932929.
    946710.
    KEGGiecj:Y75_p2174.
    eco:b2213.
    PATRICi32119785. VBIEscCol129921_2302.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M10211 Genomic DNA. Translation: AAA23412.1 .
    M10315 Genomic DNA. Translation: AAA23413.1 .
    U00008 Genomic DNA. Translation: AAA16408.1 .
    U00096 Genomic DNA. Translation: AAC75273.1 .
    AP009048 Genomic DNA. Translation: BAA15996.1 .
    J02607 Genomic DNA. Translation: AAA23415.1 .
    M13155 Genomic DNA. Translation: AAA23418.1 .
    M13828 Genomic DNA. Translation: AAA23417.1 .
    PIRi C64991. XYECO2.
    RefSeqi NP_416717.1. NC_000913.3.
    YP_490451.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ADN NMR - A 1-92 [» ]
    1EYF NMR - A 1-92 [» ]
    1SFE X-ray 2.10 A 175-354 [» ]
    1U8B X-ray 2.10 A 9-139 [» ]
    1WPK NMR - A 1-146 [» ]
    1ZGW NMR - A 1-139 [» ]
    ProteinModelPortali P06134.
    SMRi P06134. Positions 1-146, 187-351.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-9055N.
    IntActi P06134. 13 interactions.
    MINTi MINT-1310041.
    STRINGi 511145.b2213.

    Protein family/group databases

    AraC-XylS Search...

    Proteomic databases

    PRIDEi P06134.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75273 ; AAC75273 ; b2213 .
    BAA15996 ; BAA15996 ; BAA15996 .
    GeneIDi 12932929.
    946710.
    KEGGi ecj:Y75_p2174.
    eco:b2213.
    PATRICi 32119785. VBIEscCol129921_2302.

    Organism-specific databases

    EchoBASEi EB0028.
    EcoGenei EG10029. ada.

    Phylogenomic databases

    eggNOGi COG2169.
    HOGENOMi HOG000244139.
    KOi K10778.
    OMAi GMRPRQY.
    OrthoDBi EOG6WMJ4F.
    PhylomeDBi P06134.

    Enzyme and pathway databases

    BioCyci EcoCyc:PD00230.
    ECOL316407:JW2201-MONOMER.
    MetaCyc:PD00230.

    Miscellaneous databases

    EvolutionaryTracei P06134.
    PROi P06134.

    Gene expression databases

    Genevestigatori P06134.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    1.10.10.60. 1 hit.
    3.40.10.10. 1 hit.
    InterProi IPR004026. Ada_DNA_repair_Zn-bd.
    IPR016221. Bifunct_regulatory_prot_Ada.
    IPR009057. Homeodomain-like.
    IPR018060. HTH_AraC.
    IPR018062. HTH_AraC-typ_CS.
    IPR001497. MethylDNA_cys_MeTrfase_AS.
    IPR014048. MethylDNA_cys_MeTrfase_DNA-bd.
    IPR008332. MethylG_MeTrfase_N.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF02805. Ada_Zn_binding. 1 hit.
    PF01035. DNA_binding_1. 1 hit.
    PF00165. HTH_AraC. 2 hits.
    PF02870. Methyltransf_1N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000409. Ada. 1 hit.
    SMARTi SM00342. HTH_ARAC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46689. SSF46689. 1 hit.
    SSF46767. SSF46767. 1 hit.
    SSF53155. SSF53155. 1 hit.
    SSF57884. SSF57884. 1 hit.
    TIGRFAMsi TIGR00589. ogt. 1 hit.
    PROSITEi PS00041. HTH_ARAC_FAMILY_1. 2 hits.
    PS01124. HTH_ARAC_FAMILY_2. 1 hit.
    PS00374. MGMT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Purification and structure of the intact Ada regulatory protein of Escherichia coli K12, O6-methylguanine-DNA methyltransferase."
      Nakabeppu Y., Kondo H., Kawabata S., Iwanaga S., Sekiguchi M.
      J. Biol. Chem. 260:7281-7288(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: K12.
    2. "Active site and complete sequence of the suicidal methyltransferase that counters alkylation mutagenesis."
      Demple B., Sedgwick B., Robins P., Totty N., Waterfield M.D., Lindahl T.
      Proc. Natl. Acad. Sci. U.S.A. 82:2688-2692(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: B.
    3. "Automated multiplex sequencing of the E.coli genome."
      Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K., Church G.M.
      Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / BHB2600.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    7. "Induction and autoregulation of ada, a positively acting element regulating the response of Escherichia coli K-12 to methylating agents."
      Lemotte P.K., Walker G.C.
      J. Bacteriol. 161:888-895(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49.
      Strain: K12.
    8. "Structure and expression of the alkB gene of Escherichia coli related to the repair of alkylated DNA."
      Kondo H., Nakabeppu Y., Kataoka H., Kuhara S., Kawabata S., Sekiguchi M.
      J. Biol. Chem. 261:15772-15777(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 287-354.
    9. "The intracellular signal for induction of resistance to alkylating agents in E. coli."
      Teo I., Sedgwick B., Kilpatrick M.W., McCarthy T.V., Lindahl T.
      Cell 45:315-324(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
    10. "Regulatory mechanisms for induction of synthesis of repair enzymes in response to alkylating agents: ada protein acts as a transcriptional regulator."
      Nakabeppu Y., Sekiguchi M.
      Proc. Natl. Acad. Sci. U.S.A. 83:6297-6301(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
    11. "Methyl phosphotriesters in alkylated DNA are repaired by the Ada regulatory protein of E. coli."
      McCarthy T.V., Lindahl T.
      Nucleic Acids Res. 13:2683-2698(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    12. "Functional domains and methyl acceptor sites of the Escherichia coli Ada protein."
      Sedgwick B., Robins P., Totty N., Lindahl T.
      J. Biol. Chem. 263:4430-4433(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN.
    13. "Zinc binding by the methylation signaling domain of the Escherichia coli Ada protein."
      Myers L.C., Terranova M.P., Nash H.M., Markus M.A., Verdine G.L.
      Biochemistry 31:4541-4547(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: ZINC-BINDING.
    14. "Specificities of human, rat and E. coli O6-methylguanine-DNA methyltransferases towards the repair of O6-methyl and O6-ethylguanine in DNA."
      Liem L.-K., Lim A., Li B.F.L.
      Nucleic Acids Res. 22:1613-1619(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    15. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    16. "Folding topology and DNA binding of the N-terminal fragment of Ada protein."
      Sakashita H., Sakuma T., Ohkubo T., Kainosho M., Sakumi K., Sekiguchi M., Morikawa K.
      FEBS Lett. 323:252-256(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-129.
    17. "Repair of DNA methylphosphotriesters through a metalloactivated cysteine nucleophile."
      Myers L.C., Terranova M.P., Ferentz A.E., Wagner G., Verdine G.L.
      Science 261:1164-1167(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-92 IN COMPLEX WITH ZINC IONS.
    18. "Crystal structure of a suicidal DNA repair protein: the Ada O6-methylguanine-DNA methyltransferase from E. coli."
      Moore M.H., Gulbis J.M., Dodson E.J., Demple B., Moody P.C.E.
      EMBO J. 13:1495-1501(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 175-354.
      Strain: B.
    19. "Structural basis for the functional switch of the E. coli Ada protein."
      Lin Y., Doetsch V., Wintner T., Peariso K., Myers L.C., Penner-Hahn J.E., Verdine G.L., Wagner G.
      Biochemistry 40:4261-4271(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-92 IN COMPLEX WITH ZINC IONS, INTERACTION WITH DNA.
    20. "A methylation-dependent electrostatic switch controls DNA repair and transcriptional activation by E. coli ada."
      He C., Hus J.-C., Sun L.J., Zhou P., Norman D.P.G., Doetsch V., Wei H., Gross J.D., Lane W.S., Wagner G., Verdine G.L.
      Mol. Cell 20:117-129(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 9-139 IN COMPLEX WITH DNA AND ZINC IONS, STRUCTURE BY NMR OF 9-139, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE.
    21. "The solution structure of the methylated form of the N-terminal 16-kDa domain of Escherichia coli Ada protein."
      Takinowaki H., Matsuda Y., Yoshida T., Kobayashi Y., Ohkubo T.
      Protein Sci. 15:487-497(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-146 IN COMPLEX WITH ZINC IONS, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE CYS-38.

    Entry informationi

    Entry nameiADA_ECOLI
    AccessioniPrimary (citable) accession number: P06134
    Secondary accession number(s): Q47032
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: February 1, 1994
    Last modified: October 1, 2014
    This is version 159 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    This enzyme catalyzes only one turnover and therefore is not strictly catalytic. According to one definition, an enzyme is a biocatalyst that acts repeatedly and over many reaction cycles.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3