P0AB84 (END3_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endonuclease III
EC=4.2.99.18

Alternative name(s):
DNA-(apurinic or apyrimidinic site) lyase

Gene names

Name:	nth
Ordered Locus Names:	c2025

Organism

Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) [Complete proteome] [HAMAP]

Taxonomic identifier

199310 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	211 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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 By similarity. HAMAP-Rule MF_00942
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. HAMAP-Rule MF_00942
Cofactor	Binds 1 4Fe-4S cluster By similarity.
Sequence similarities	Belongs to the Nth/MutY family. Contains 1 HhH domain.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Ligand	4Fe-4S DNA-binding Iron Iron-sulfur Metal-binding
Molecular function	Glycosidase Hydrolase Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	base-excision repair Inferred from electronic annotation. Source: InterPro
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Inferred from electronic annotation. Source: UniProtKB-KW DNA-(apurinic or apyrimidinic site) lyase activity Inferred from electronic annotation. Source: EC endonuclease activity Inferred from electronic annotation. Source: InterPro hydrolase activity, acting on glycosyl bonds Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 211	211	Endonuclease III HAMAP-Rule MF_00942		PRO_0000102211
Regions
	Domain	108 – 127	20	HhH
Sites
	Metal binding	187	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	194	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	197	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	203	1	Iron-sulfur (4Fe-4S)

Sequences

	Sequence		Length	Mass (Da)
	P0AB84 [UniParc]. Last modified November 8, 2005. Version 1. Checksum: FF4245823B7F902B	FASTA	211	23,562
	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

References

[1]

"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CFT073 / ATCC 700928 / UPEC.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014075 Genomic DNA. Translation: AAN80485.1.
RefSeq	NP_753920.1. NC_004431.1.
3D structure databases
ProteinModelPortal	P0AB84.
SMR	P0AB84. Positions 1-211.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1223364.
STRING	199310.c2025.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAN80485; AAN80485; c2025.
GeneID	1036116.
KEGG	ecc:c2025.
PATRIC	18281947. VBIEscCol75197_1892.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000252206.
KO	K10773.
OMA	NNKSKHL.
ProtClustDB	PRK10702.
Family and domain databases
Gene3D	1.10.1670.10. 1 hit. 1.10.340.30. 1 hit.
HAMAP	MF_00942. Nth.
InterPro	IPR011257. DNA_glycosylase. IPR004036. Endonuclease-III_CS2. IPR005759. Endonuclease-III_Nth. 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. [Graphical view]
Pfam	PF10576. EndIII_4Fe-2S. 1 hit. PF00633. HHH. 1 hit. PF00730. HhH-GPD. 1 hit. [Graphical view]
PIRSF	PIRSF001435. Nth. 1 hit.
SMART	SM00478. ENDO3c. 1 hit. SM00525. FES. 1 hit. SM00278. HhH1. 1 hit. [Graphical view]
SUPFAM	SSF48150. DNA_glycsylse. 1 hit.
TIGRFAMs	TIGR01083. nth. 1 hit.
PROSITE	PS00764. ENDONUCLEASE_III_1. 1 hit. PS01155. ENDONUCLEASE_III_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

END3_ECOL6

Accession

Primary (citable) accession number: P0AB84
Secondary accession number(s): P20625

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	November 8, 2005
Last modified:	May 1, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program