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P0A6C1 (END4_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endonuclease 4

EC=3.1.21.2
Alternative name(s):
Endodeoxyribonuclease IV
Endonuclease IV
Gene names
Name:nfo
Ordered Locus Names:b2159, JW2146
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length285 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) to produce new 5'-ends that are base-free deoxyribose 5-phosphate residues. It preferentially attacks modified AP sites created by bleomycin and neocarzinostatin. HAMAP-Rule MF_00152

Catalytic activity

Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products. HAMAP-Rule MF_00152

Cofactor

Binds 3 zinc ions. Can also bind manganese.

Subunit structure

Monomer.

Induction

Endonuclease IV is induced by agents which generate superoxide radical anions. HAMAP-Rule MF_00152

Sequence similarities

Belongs to the AP endonuclease 2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 285285Endonuclease 4 HAMAP-Rule MF_00152
PRO_0000190838

Sites

Metal binding691Zinc 1
Metal binding1091Zinc 1
Metal binding1451Zinc 1
Metal binding1451Zinc 2
Metal binding1791Zinc 2
Metal binding1821Zinc 3
Metal binding2161Zinc 2
Metal binding2291Zinc 3
Metal binding2311Zinc 3
Metal binding2611Zinc 2

Experimental info

Sequence conflict101A → R in AAA24216. Ref.1
Sequence conflict2731A → T in AAA60529. Ref.2

Secondary structure

................................................. 285
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A6C1 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: EAAE5861E54C47FD

FASTA28531,480
        10         20         30         40         50         60 
MKYIGAHVSA AGGLANAAIR AAEIDATAFA LFTKNQRQWR AAPLTTQTID EFKAACEKYH 

        70         80         90        100        110        120 
YTSAQILPHD SYLINLGHPV TEALEKSRDA FIDEMQRCEQ LGLSLLNFHP GSHLMQISEE 

       130        140        150        160        170        180 
DCLARIAESI NIALDKTQGV TAVIENTAGQ GSNLGFKFEH LAAIIDGVED KSRVGVCIDT 

       190        200        210        220        230        240 
CHAFAAGYDL RTPAECEKTF ADFARTVGFK YLRGMHLNDA KSTFGSRVDR HHSLGEGNIG 

       250        260        270        280 
HDAFRWIMQD DRFDGIPLIL ETINPDIWAE EIAWLKAQQT EKAVA 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the nfo gene of Escherichia coli K-12."
Saporito S.M., Cunningham R.P.
J. Bacteriol. 170:5141-5145(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"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.
[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]"Metalloenzymes in DNA repair. Escherichia coli endonuclease IV and Saccharomyces cerevisiae Apn1."
Levin J.D., Shapiro R., Demple B.
J. Biol. Chem. 266:22893-22898(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: METAL-BINDING STUDIES.
[6]"Structure of the DNA repair enzyme endonuclease IV and its DNA complex: double-nucleotide flipping at abasic sites and three-metal-ion catalysis."
Hosfield D.J., Guan Y., Haas B.J., Cunningham R.P., Tainer J.A.
Cell 98:397-408(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.02 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M22591 Genomic DNA. Translation: AAA24216.1.
U00007 Genomic DNA. Translation: AAA60529.1.
U00096 Genomic DNA. Translation: AAC75220.1.
AP009048 Genomic DNA. Translation: BAE76636.1.
PIRNDEC4. F64984.
RefSeqNP_416664.1. NC_000913.3.
YP_490398.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QTWX-ray1.02A1-285[»]
1QUMX-ray1.55A1-285[»]
2NQ9X-ray1.45A1-285[»]
2NQHX-ray1.10A1-285[»]
2NQJX-ray2.45A/B1-285[»]
4K1GX-ray1.90A/B1-285[»]
ProteinModelPortalP0A6C1.
SMRP0A6C1. Positions 1-285.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-47966N.
IntActP0A6C1. 10 interactions.
MINTMINT-1242700.
STRING511145.b2159.

Chemistry

ChEMBLCHEMBL1293285.

Proteomic databases

PaxDbP0A6C1.
PRIDEP0A6C1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75220; AAC75220; b2159.
BAE76636; BAE76636; BAE76636.
GeneID12932805.
946669.
KEGGecj:Y75_p2121.
eco:b2159.
PATRIC32119667. VBIEscCol129921_2244.

Organism-specific databases

EchoBASEEB0645.
EcoGeneEG10651. nfo.

Phylogenomic databases

eggNOGCOG0648.
HOGENOMHOG000224893.
KOK01151.
OMAINLGHPD.
OrthoDBEOG6Z0QCM.
PhylomeDBP0A6C1.
ProtClustDBPRK01060.

Enzyme and pathway databases

BioCycEcoCyc:EG10651-MONOMER.
ECOL316407:JW2146-MONOMER.
MetaCyc:EG10651-MONOMER.
BRENDA3.1.21.2. 2026.

Gene expression databases

GenevestigatorP0A6C1.

Family and domain databases

Gene3D3.20.20.150. 1 hit.
HAMAPMF_00152. Nfo.
InterProIPR001719. AP_endonuc_2.
IPR018246. AP_endonuc_F2_Zn_BS.
IPR013022. Xyl_isomerase-like_TIM-brl.
[Graphical view]
PANTHERPTHR21445. PTHR21445. 1 hit.
PfamPF01261. AP_endonuc_2. 1 hit.
[Graphical view]
SMARTSM00518. AP2Ec. 1 hit.
[Graphical view]
SUPFAMSSF51658. SSF51658. 1 hit.
TIGRFAMsTIGR00587. nfo. 1 hit.
PROSITEPS00729. AP_NUCLEASE_F2_1. 1 hit.
PS00730. AP_NUCLEASE_F2_2. 1 hit.
PS00731. AP_NUCLEASE_F2_3. 1 hit.
PS51432. AP_NUCLEASE_F2_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A6C1.
PROP0A6C1.

Entry information

Entry nameEND4_ECOLI
AccessionPrimary (citable) accession number: P0A6C1
Secondary accession number(s): P12638, P78086, Q2MAS0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: April 16, 2014
This is version 88 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