Endonuclease III - Mycobacterium tuberculosis

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P63540 (END3_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 67. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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:	Rv3674c, MT3775
ORF Names:	MTV025.022c

Organism

Mycobacterium tuberculosis [Reference proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	245 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. Has a preference for oxidized pyrimidines, such as thymine glycol (prefers 5S isomers) 5,6-dihydrouracil:G, 5-hydroxyuracil:G, 5-hydroxycytosine:G and urea:A. Cleaves ssDNA containing an AP site. Ref.3
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.
Sequence caution	The sequence AAK48142.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

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 Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from direct assay Ref.3. Source: MTBBASE base-excision repair Inferred from electronic annotation. Source: InterPro
Cellular_component	cell wall Inferred from direct assay PubMed 15525680. Source: MTBBASE plasma membrane Inferred from direct assay PubMed 15525680. Source: MTBBASE
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW DNA N-glycosylase activity Inferred from direct assay Ref.3. Source: MTBBASE DNA-(apurinic or apyrimidinic site) lyase activity Inferred from electronic annotation. Source: EC double-stranded DNA binding Inferred from direct assay Ref.3. Source: MTBBASE endonuclease activity Inferred from electronic annotation. Source: InterPro 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 – 245

245

Endonuclease III HAMAP-Rule MF_00942

PRO_0000102219

Regions

Domain

119 – 138

HhH

Sites

Metal binding

198

Iron-sulfur (4Fe-4S) By similarity

Metal binding

205

Iron-sulfur (4Fe-4S) By similarity

Metal binding

208

Iron-sulfur (4Fe-4S) By similarity

Metal binding

214

Iron-sulfur (4Fe-4S) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P63540 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 2B6D16195DD090DE
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FASTA

245

27,030

        10         20         30         40         50         60 
MPGRWSAETR LALVRRARRM NRALAQAFPH VYCELDFTTP LELAVATILS AQSTDKRVNL 

        70         80         90        100        110        120 
TTPALFARYR TARDYAQADR TELESLIRPT GFYRNKAASL IGLGQALVER FGGEVPATMD 

       130        140        150        160        170        180 
KLVTLPGVGR KTANVILGNA FGIPGITVDT HFGRLVRRWR WTTAEDPVKV EQAVGELIER 

       190        200        210        220        230        240 
KEWTLLSHRV IFHGRRVCHA RRPACGVCVL AKDCPSFGLG PTEPLLAAPL VQGPETDHLL 


ALAGL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. Barrell B.G. Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"The oxidative DNA glycosylases of Mycobacterium tuberculosis exhibit different substrate preferences from their Escherichia coli counterparts." Guo Y., Bandaru V., Jaruga P., Zhao X., Burrows C.J., Iwai S., Dizdaroglu M., Bond J.P., Wallace S.S. DNA Repair 9:177-190(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. Strain: ATCC 25618 / H37Rv.
[4]	"Base excision and nucleotide excision repair pathways in mycobacteria." Kurthkoti K., Varshney U. Tuberculosis 91:533-543(2011) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX842583 Genomic DNA. Translation: CAA17996.2. AE000516 Genomic DNA. Translation: AAK48142.1. Different initiation. AL123456 Genomic DNA. Translation: CCP46497.1.
PIR	C70790.
RefSeq	NP_218191.2. NC_000962.3. NP_338328.1. NC_002755.2. YP_006517162.1. NC_018143.1.
3D structure databases
ProteinModelPortal	P63540.
SMR	P63540. Positions 24-241.
ModBase	Search...
Protein-protein interaction databases
STRING	83332.Rv3674c.
Proteomic databases
PRIDE	P63540.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAK48142; AAK48142; MT3775.
GeneID	13317283. 885058. 926474.
KEGG	mtc:MT3775. mtu:Rv3674c. mtv:RVBD_3674c.
PATRIC	18130064. VBIMycTub22151_4125.
Organism-specific databases
TubercuList	Rv3674c.
Phylogenomic databases
eggNOG	COG0177.
HOGENOM	HOG000252208.
KO	K10773.
OMA	NNKSKHL.
ProtClustDB	CLSK799395.
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. 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_MYCTU

Accession

Primary (citable) accession number: P63540
Secondary accession number(s): L0TEW4, O69642

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents