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P06134

- ADA_ECOLI

UniProt

P06134 - ADA_ECOLI

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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

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

Zn2+Note: Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei34 – 341DNA1 Publication
Active sitei38 – 381Nucleophile; methyl group acceptor from methylphosphotriester1 PublicationPROSITE-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. sequence-specific DNA binding Source: InterPro
  3. sequence-specific DNA binding transcription factor activity Source: InterPro
  4. 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
Complete GO annotation...

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 – 63Combined sources
Helixi9 – 179Combined sources
Helixi21 – 233Combined sources
Turni24 – 263Combined sources
Beta strandi27 – 315Combined sources
Turni32 – 343Combined sources
Beta strandi36 – 383Combined sources
Helixi49 – 513Combined sources
Beta strandi52 – 576Combined sources
Helixi58 – 636Combined sources
Beta strandi67 – 693Combined sources
Turni70 – 723Combined sources
Beta strandi76 – 783Combined sources
Helixi79 – 9315Combined sources
Beta strandi96 – 983Combined sources
Helixi102 – 1098Combined sources
Helixi113 – 12311Combined sources
Helixi128 – 13710Combined sources
Turni142 – 1443Combined sources
Beta strandi190 – 1967Combined sources
Beta strandi199 – 2057Combined sources
Beta strandi207 – 21711Combined sources
Helixi219 – 22911Combined sources
Helixi240 – 25415Combined sources
Beta strandi255 – 2573Combined sources
Helixi270 – 27910Combined sources
Helixi290 – 2967Combined sources
Helixi303 – 3119Combined sources
Helixi321 – 3233Combined sources
Helixi338 – 34811Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP06134.
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

        10         20         30         40         50
MKKATCLTDD QRWQSVLARD PNADGEFVFA VRTTGIFCRP SCRARHALRE
60 70 80 90 100
NVSFYANASE ALAAGFRPCK RCQPEKANAQ QHRLDKITHA CRLLEQETPV
110 120 130 140 150
TLEALADQVA MSPFHLHRLF KATTGMTPKA WQQAWRARRL RESLAKGESV
160 170 180 190 200
TTSILNAGFP DSSSYYRKAD ETLGMTAKQF RHGGENLAVR YALADCELGR
210 220 230 240 250
CLVAESERGI CAILLGDDDA TLISELQQMF PAADNAPADL MFQQHVREVI
260 270 280 290 300
ASLNQRDTPL TLPLDIRGTA FQQQVWQALR TIPCGETVSY QQLANAIGKP
310 320 330 340 350
KAVRAVASAC AANKLAIIIP CHRVVRGDGT LSGYRWGVSR KAQLLRREAE

NEER
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P06134.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 161 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