Reviewed, UniProtKB/Swiss-Prot O05956 (END3_RICPR)

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:	RP746

Organism

Rickettsia prowazekii [Complete proteome] [HAMAP]

Taxonomic identifier

782 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › typhus group

Protein attributes

Sequence length	212 AA.
Sequence status	Complete.
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 – 212	212	Endonuclease III		PRO_0000102221
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)
	O05956-1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: A7FDA4F6033A6382	FASTA	212	24,174
	10 20 30 40 50 60 MQAQIMNKIF EIFSKNNPKP QTELIYKNDF TLLVAVILSA RATDISVNLA TKHLFETYNT 70 80 90 100 110 120 PEKFLELGEE GLKKYIKSIG LFNSKAKNII ALCQILIKNY QTSIPNNFKE LVKLPGVGRK 130 140 150 160 170 180 TANVVLNCLF AMPTMAVDTH VFRVSKRIGL AKGNTAAIVE KELLQIIDEK WLTYAHHWLI 190 200 210 LHGRYICKAR KPGCNICPIK EYCEYYINTF SS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genomic rearrangements during evolution of the obligate intracellular parasite Rickettsia prowazekii as inferred from an analysis of 52015 bp nucleotide sequence." Andersson J.O., Andersson S.G.E. Microbiology 143:2783-2795(1997) [PubMed: 9274032] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Madrid E.
[2]	"The genome sequence of Rickettsia prowazekii and the origin of mitochondria." Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., Kurland C.G. Nature 396:133-140(1998) [PubMed: 9823893] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Madrid E.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y11778 Genomic DNA. Translation: CAA72458.1. AJ235273 Genomic DNA. Translation: CAA15174.1.
PIR	F71634.
RefSeq	NP_221098.1.
3D structure databases
SMR	O05956. Positions 7-208.
ModBase	Search...
Genome annotation databases
GeneID	883968.
KEGG	rpr:RP746.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG464473.
OMA	EPTIAVD.
Enzyme and pathway databases
BioCyc	RPRO272947:RP746-MONOMER.
BRENDA	4.2.99.18. 141977.
Family and domain databases
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. [Graphical view]
Pfam	PF10576. EndIII_4Fe-2S. 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_RICPR

Accession

Primary (citable) accession number: O05956

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 1, 1997
Last modified:	February 9, 2010
This is version 66 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)