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Reviewed, UniProtKB/Swiss-Prot P0AB83 (END3_ECOLI)

Last modified June 16, 2009. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length211 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Has both an apurinic and/or apyrimidinic endonuclease activity and a DNA N-glycosylase activity. Incises damaged DNA at cytosines, thymines and guanines. Acts on a damaged strand, 5' from the damaged site. Required for the repair of both oxidative DNA damage and spontaneous mutagenic lesions.

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.

Cofactor

Binds 1 4Fe-4S cluster. The cluster is not important for the catalytic activity, but which is probably involved in the proper positioning of the enzyme along the DNA strand.

Subunit structure

Monomer.

Sequence similarities

Belongs to the nth/mutY family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

aceEP0AFG81EBI-555213,EBI-542683

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 211211Endonuclease III
PRO_0000102210

Sites

Active site1121Nucleophile; for N-glycosylase activity Probable
Metal binding1871Iron-sulfur (4Fe-4S)
Metal binding1941Iron-sulfur (4Fe-4S)
Metal binding1971Iron-sulfur (4Fe-4S)
Metal binding2031Iron-sulfur (4Fe-4S)

Experimental info

Mutagenesis1201K → Q: 10000-fold decrease in activity. Ref.5

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AB83-1 [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: 2669955] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10.
[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: 9097039] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"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: 8092678] [Abstract]
Cited for: MUTAGENESIS OF LYS-120.
[6]"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: 1411536] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[7]"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: 7664751] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).

Cross-references

Sequence databases

J02857 Genomic DNA. Translation: AAA24227.1.
U00096 Genomic DNA. Translation: AAC74705.1.
AP009048 Genomic DNA. Translation: BAA15387.1.
PIRA32412.
RefSeqAP_002255.1.
NP_416150.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2ABKX-ray1.85A1-211[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP0AB83. 6 interactions.

Genome annotation databases

GeneID947122.
GenomeReviewsGene locus JW1625 in contig AP009048_GR.
Gene locus b1633 in contig U00096_GR.
KEGGecj:JW1625.
eco:b1633.

Organism-specific databases

EchoBASEEB0656.
EcoGeneEG10662. nth.
CMRSearch...

Phylogenomic databases

HOGENOMP0AB83.
OMAP0AB83. EPTIAVD.

Enzyme and pathway databases

BioCycEcoCyc:EG10662-MON.

Family and domain databases

InterProIPR004036. Endonuclease-III_CS2.
IPR005759. Endonuclease-III_Nth.
IPR004035. Endouclease-III_FeS-bd_CS1.
IPR003651. Endouclease3-like_FeS-loop.
IPR003583. Helix-hairpin-helix_DNA-bd.
IPR003265. HhH-GPD_domain.
IPR000445. HhH_motif.
[Graphical view]
PfamPF10576. EndIII_4Fe-2S. 1 hit.
PF00633. HHH. 1 hit.
PF00730. HhH-GPD. 1 hit.
[Graphical view]
SMARTSM00478. ENDO3c. 1 hit.
SM00525. FES. 1 hit.
SM00278. HhH1. 1 hit.
[Graphical view]
TIGRFAMsTIGR01083. nth. 1 hit.
PROSITEPS00764. ENDONUCLEASE_III_1. 1 hit.
PS01155. ENDONUCLEASE_III_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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: June 16, 2009
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents