Reviewed, UniProtKB/Swiss-Prot P0AB84 (END3_ECOL6)

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 [Complete proteome] [HAMAP]

Taxonomic identifier

217992 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	211 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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 By similarity.
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 By similarity.
Subunit structure	Monomer By similarity.
Sequence similarities	Belongs to the nth/mutY family.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Ligand	4Fe-4S 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
Cellular component	intracellular 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: InterPro 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 iron 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		PRO_0000102211
Sites
	Active site	112	1	Nucleophile; for N-glycosylase activity By similarity
	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)
	P0AB84-1 [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: 12471157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014075 Genomic DNA. Translation: AAN80485.1.
RefSeq	NP_753920.1.
3D structure databases
SMR	P0AB84. Positions 1-211.
ModBase	Search...
Genome annotation databases
GeneID	1036116.
GenomeReviews	Gene locus c2025 in contig AE014075_GR.
KEGG	ecc:c2025.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P0AB84.
OMA	P0AB84. EPTIAVD.
Enzyme and pathway databases
BRENDA	4.2.99.18. 292881.
Family and domain databases
InterPro	IPR004036. 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]
Pfam	PF10576. EndIII_4Fe-2S. 1 hit. PF00633. HHH. 1 hit. PF00730. HhH-GPD. 1 hit. [Graphical view]
SMART	SM00478. ENDO3c. 1 hit. SM00525. FES. 1 hit. SM00278. HhH1. 1 hit. [Graphical view]
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:	June 16, 2009
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)