O83754 (END3_TREPA) 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:	TP_0775

Organism

Treponema pallidum (strain Nichols) [Complete proteome] [HAMAP]

Taxonomic identifier

243276 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Spirochaetes › Spirochaetia › Spirochaetales › Spirochaetaceae › Treponema › Treponema pallidum › Treponema pallidum subsp. pallidum

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_0000102225
Regions
	Domain	111 – 130	20	HhH
Sites
	Metal binding	190	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	197	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	200	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	206	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	O83754 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: E6CA4C35DA370BAD	FASTA	211	23,419
	10 20 30 40 50 60 MRLLDSKGVH AVFEQLHAAN PQPQGELHWR NTFTLLVAVL LSAQATDKSV NKATAALFDV 70 80 90 100 110 120 ADTPQAMLAL GEERLCSYIR TINLYPTKAR RIIALSAELI ERFAAQVPCD AHALESLPGV 130 140 150 160 170 180 GHKTANVVLN MGFGIPTIAV DTHILRTAPR IGLSSGRTPR AVERDLLVVT PREFRMHAHH 190 200 210 WILLHGRYTC TARRPRCTEC CLRDLCCKNN I

References

[1]

"Complete genome sequence of Treponema pallidum, the syphilis spirochete." Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G., Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A., Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D., Khalak H.G., Richardson D.L., Howell J.K. , Chidambaram M., Utterback T.R., McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A., Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O., Venter J.C. Science 281:375-388(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Nichols.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000520 Genomic DNA. Translation: AAC65744.1.
PIR	H71281.
RefSeq	NP_219212.1. NC_000919.1.
3D structure databases
ProteinModelPortal	O83754.
SMR	O83754. Positions 7-208.
ModBase	Search...
Protein-protein interaction databases
STRING	243276.TP0775.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC65744; AAC65744; TP_0775.
GeneID	2611450.
KEGG	tpa:TP0775.
PATRIC	20531643. VBITrePal57110_0819.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0177.
KO	K10773.
OMA	NNKSKHL.
ProtClustDB	CLSK493747.
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. IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif. IPR023170. HTH_base_excis_C. [Graphical view]
Pfam	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_TREPA

Accession

Primary (citable) accession number: O83754

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1998
Last modified:	May 1, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program