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P0AB83 (END3_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endonuclease III

EC=4.2.99.18
Alternative name(s):
DNA-(apurinic or apyrimidinic site) lyase
Gene names
Name:nth
Ordered Locus Names:b1633, JW1625
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length211 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. Ref.1 Ref.5 Ref.6

Catalytic activity

The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. Ref.6

Cofactor

Binds 1 4Fe-4S cluster. The cluster does not appear to play a role in catalysis, but is probably involved in DNA-binding and proper positioning of the enzyme along the DNA strand. Ref.7 Ref.9

Subunit structure

Monomer. Ref.5

Sequence similarities

Belongs to the Nth/MutY family.

Contains 1 HhH domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

aceEP0AFG82EBI-555213,EBI-542683

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 211211Endonuclease III HAMAP-Rule MF_00942
PRO_0000102210

Regions

Domain108 – 12720HhH

Sites

Metal binding1871Iron-sulfur (4Fe-4S)
Metal binding1941Iron-sulfur (4Fe-4S)
Metal binding1971Iron-sulfur (4Fe-4S)
Metal binding2031Iron-sulfur (4Fe-4S)

Experimental info

Mutagenesis1201K → Q: 100000-fold decrease in activity and slight decrease in substrate affinity. Ref.9
Mutagenesis1381D → N: 100-fold decrease in activity and 4-fold increase in substrate affinity. Ref.9
Mutagenesis1911K → E: Slight decrease in activity and 130-fold increase in substrate affinity. Ref.9

Secondary structure

................................ 211
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AB83 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: FF4245823B7F902B

FASTA21123,562
        10         20         30         40         50         60 
MNKAKRLEIL TRLRENNPHP TTELNFSSPF ELLIAVLLSA QATDVSVNKA TAKLYPVANT 

        70         80         90        100        110        120 
PAAMLELGVE GVKTYIKTIG LYNSKAENII KTCRILLEQH NGEVPEDRAA LEALPGVGRK 

       130        140        150        160        170        180 
TANVVLNTAF GWPTIAVDTH IFRVCNRTQF APGKNVEQVE EKLLKVVPAE FKVDCHHWLI 

       190        200        210 
LHGRYTCIAR KPRCGSCIIE DLCEYKEKVD I 

« Hide

References

« Hide 'large scale' references
[1]"Purification and characterization of Escherichia coli endonuclease III from the cloned nth gene."
Asahara H., Wistort P.M., Bank J.F., Bakerian R.H., Cunningham R.P.
Biochemistry 28:4444-4449(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, FUNCTION.
[2]"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"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.
[5]"DNA glycosylase activities for thymine residues damaged by ring saturation, fragmentation, or ring contraction are functions of endonuclease III in Escherichia coli."
Breimer L.H., Lindahl T.
J. Biol. Chem. 259:5543-5548(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[6]"The mechanisms of action of E. coli endonuclease III and T4 UV endonuclease (endonuclease V) at AP sites."
Kim J., Linn S.
Nucleic Acids Res. 16:1135-1141(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
[7]"Structure and function of Escherichia coli endonuclease III."
Cunningham R.P., Ahern H., Xing D., Thayer M.M., Tainer J.A.
Ann. N. Y. Acad. Sci. 726:215-222(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: COFACTOR.
[8]"Atomic structure of the DNA repair [4Fe-4S] enzyme endonuclease III."
Kuo C.-F., McRee D., Fisher C.L., O'Handley S.F., Cunningham R.P., Tainer J.A.
Science 258:434-440(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[9]"Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure."
Thayer M.M., Ahern H., Xing D., Cunningham R.P., Tainer J.A.
EMBO J. 14:4108-4120(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), COFACTOR, DNA-BINDING, MUTAGENESIS OF LYS-120; ASP-138 AND LYS-191.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02857 Genomic DNA. Translation: AAA24227.1.
U00096 Genomic DNA. Translation: AAC74705.1.
AP009048 Genomic DNA. Translation: BAA15387.1.
PIRA32412.
RefSeqNP_416150.1. NC_000913.3.
YP_489897.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ABKX-ray1.85A1-211[»]
ProteinModelPortalP0AB83.
SMRP0AB83. Positions 1-211.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48071N.
IntActP0AB83. 6 interactions.
MINTMINT-1223379.
STRING511145.b1633.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74705; AAC74705; b1633.
BAA15387; BAA15387; BAA15387.
GeneID12933192.
947122.
KEGGecj:Y75_p1610.
eco:b1633.
PATRIC32118568. VBIEscCol129921_1704.

Organism-specific databases

EchoBASEEB0656.
EcoGeneEG10662. nth.

Phylogenomic databases

eggNOGCOG0177.
HOGENOMHOG000252206.
KOK10773.
OMANNKSKHL.
OrthoDBEOG6H4KC5.
PhylomeDBP0AB83.
ProtClustDBPRK10702.

Enzyme and pathway databases

BioCycEcoCyc:EG10662-MONOMER.
ECOL316407:JW1625-MONOMER.
MetaCyc:EG10662-MONOMER.

Gene expression databases

GenevestigatorP0AB83.

Family and domain databases

Gene3D1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
HAMAPMF_00942. Nth.
InterProIPR011257. DNA_glycosylase.
IPR004036. Endonuclease-III-like_CS2.
IPR004035. Endouclease-III_FeS-bd_BS.
IPR003651. Endouclease3_FeS-loop_motif.
IPR003265. HhH-GPD_domain.
IPR000445. HhH_motif.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR023170. HTH_base_excis_C.
IPR005759. Nth.
[Graphical view]
PfamPF10576. EndIII_4Fe-2S. 1 hit.
PF00633. HHH. 1 hit.
PF00730. HhH-GPD. 1 hit.
[Graphical view]
PIRSFPIRSF001435. Nth. 1 hit.
SMARTSM00478. ENDO3c. 1 hit.
SM00525. FES. 1 hit.
SM00278. HhH1. 1 hit.
[Graphical view]
SUPFAMSSF48150. SSF48150. 1 hit.
TIGRFAMsTIGR01083. nth. 1 hit.
PROSITEPS00764. ENDONUCLEASE_III_1. 1 hit.
PS01155. ENDONUCLEASE_III_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0AB83.
PROP0AB83.

Entry information

Entry nameEND3_ECOLI
AccessionPrimary (citable) accession number: P0AB83
Secondary accession number(s): P20625
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: April 16, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene