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P63540 (END3_MYCTU) Reviewed, UniProtKB/Swiss-Prot

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

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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
OrganismMycobacterium tuberculosis [Reference proteome] [HAMAP]
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length245 AA.
Sequence statusComplete.
Protein existenceInferred 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 245245Endonuclease III HAMAP-Rule MF_00942
PRO_0000102219

Regions

Domain119 – 13820HhH

Sites

Metal binding1981Iron-sulfur (4Fe-4S) By similarity
Metal binding2051Iron-sulfur (4Fe-4S) By similarity
Metal binding2081Iron-sulfur (4Fe-4S) By similarity
Metal binding2141Iron-sulfur (4Fe-4S) By similarity

Sequences

Sequence LengthMass (Da)Tools
P63540 [UniParc].

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

FASTA24527,030
        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' 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. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., 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. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., 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.
PIRC70790.
RefSeqNP_218191.2. NC_000962.3.
NP_338328.1. NC_002755.2.
YP_006517162.1. NC_018143.1.

3D structure databases

ProteinModelPortalP63540.
SMRP63540. Positions 24-241.
ModBaseSearch...

Protein-protein interaction databases

STRING83332.Rv3674c.

Proteomic databases

PRIDEP63540.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK48142; AAK48142; MT3775.
GeneID13317283.
885058.
926474.
KEGGmtc:MT3775.
mtu:Rv3674c.
mtv:RVBD_3674c.
PATRIC18130064. VBIMycTub22151_4125.

Organism-specific databases

TubercuListRv3674c.

Phylogenomic databases

eggNOGCOG0177.
HOGENOMHOG000252208.
KOK10773.
OMANNKSKHL.
ProtClustDBCLSK799395.

Family and domain databases

Gene3D1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
HAMAPMF_00942. Nth.
InterProIPR011257. 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]
PfamPF10576. EndIII_4Fe-2S. 1 hit.
PF00633. HHH. 1 hit.
PF00730. HhH-GPD. 1 hit.
[Graphical view]
PIRSFPIRSF001435. Nth. 1 hit.
SMARTSM00478. ENDO3c. 1 hit.
SM00525. FES. 1 hit.
SM00278. HhH1. 1 hit.
[Graphical view]
SUPFAMSSF48150. DNA_glycsylse. 1 hit.
TIGRFAMsTIGR01083. nth. 1 hit.
PROSITEPS00764. ENDONUCLEASE_III_1. 1 hit.
PS01155. ENDONUCLEASE_III_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameEND3_MYCTU
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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