Reviewed, UniProtKB/Swiss-Prot P57219 (END3_BUCAI)

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:	BU119

Organism

Buchnera aphidicola subsp. Acyrthosiphon pisum (Acyrthosiphon pisum symbiotic bacterium) [Complete proteome] [HAMAP]

Taxonomic identifier

118099 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	210 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 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.
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 – 210	210	Endonuclease III		PRO_0000102214
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) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P57219-1 [UniParc]. Last modified December 1, 2000. Version 1. Checksum: C43A060F24694660	FASTA	210	24,388
	10 20 30 40 50 60 MNKKKRYEIL SILSRNNPEP KIELFFSSDF ELLLSVILSA QSTDFIVNKT TKILFKIANT 70 80 90 100 110 120 PETIFLLGLE RLKNYIKDIG LYNTKALNII RTSFIILTKY NSIVPNNRIE LESLPGVGRK 130 140 150 160 170 180 TANIILNILF KKKTIAVDTH VFRVCNRTNF AKGKNVKIVE EKLIKVVPSI FKLNFHSWFI 190 200 210 LHGRYICTAR KIKCNICLIF KLCEFKQKIF

References

[1]	"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS." Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H. Nature 407:81-86(2000) [PubMed: 10993077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tokyo 1998.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000003 Genomic DNA. Translation: BAB12837.1.
RefSeq	NP_239951.1.
3D structure databases
HSSP	HSSP built from PDB template 2ABK based on UniProtKB P20625.
ModBase	Search...
Genome annotation databases
GeneID	1109563.
GenomeReviews	Gene locus BU119 in contig BA000003_GR.
KEGG	buc:BU119.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P57219.
OMA	EPTIAVD.
Enzyme and pathway databases
BioCyc	BSP107806:BU119-MON.
Family and domain databases
InterPro	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. [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. False negative. PS01155. ENDONUCLEASE_III_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

END3_BUCAI

Accession

Primary (citable) accession number: P57219

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	November 3, 2009
This is version 56 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)