Q9WYK0 (END3_THEMA) 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:	TM_0366

Organism

Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]

Taxonomic identifier

243274 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Thermotogae › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga › Thermotoga maritima

Protein attributes

Sequence length	213 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 Reference 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 – 213	213	Endonuclease III HAMAP-Rule MF_00942		PRO_0000102224
Regions
	Domain	101 – 120	20	HhH
Sites
	Metal binding	180	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	187	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	190	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	196	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9WYK0 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: D9716CD6FEFA85D4	FASTA	213	24,928
	10 20 30 40 50 60 MIEELAREIV KRFPRNHKET DPFRVLISTV LSQRTRDENT EKASKKLFEV YRTPQELAKA 70 80 90 100 110 120 KPEDLYDLIK ESGMYRQKAE RIVEISRILV EKYGGRVPDS LEELLKLPGV GRKTANIVLW 130 140 150 160 170 180 VGFKKPALAV DTHVHRISNR LGWVKTRTPE ETEEALKKLL PEDLWGPING SMVEFGRRIC 190 200 210 KPQNPLCEEC FLKNHCEFYR RRGKGEVRNR TER

References

[1]

"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima." Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Nature 399:323-329(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000512 Genomic DNA. Translation: AAD35453.1.
PIR	F72387.
RefSeq	NP_228177.1. NC_000853.1.
3D structure databases
ProteinModelPortal	Q9WYK0.
ModBase	Search...
Protein-protein interaction databases
STRING	243274.TM0366.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAD35453; AAD35453; TM_0366.
GeneID	897325.
KEGG	tma:TM0366.
PATRIC	23935613. VBITheMar51294_0371.
Phylogenomic databases
eggNOG	COG0177.
KO	K10773.
OMA	GKPGICV.
ProtClustDB	CLSK875111.
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. 2 hits. [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_THEMA

Accession

Primary (citable) accession number: Q9WYK0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program