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Protein

Endonuclease V

Gene
N/A
Organism
Enterobacteria phage T4 (Bacteriophage T4)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Participates in the repair of UV-damaged DNA by excising pyrimidine dimers that are the major UV-lesions (PubMed:6254991). DNA glycosylase activity hydrolyzes the glycosylic bond of the 5' pyrimidine of the dimer (PubMed:6254991). This leaves apurinic/apyrimidic (AP) sites in the DNA. These AP sites are removed by the AP lyase activity which cleaves the intrapyrimidine phosphodiester bond (PubMed:6254991). Catalysis proceeds via a protonated imine covalent intermediate between the alpha-amino group of the N-terminal threonine residue and the C1' of the deoxyribose sugar of the 5' pyrimidine at the dimer site (PubMed:8347626) (PubMed:16916523).3 Publications

Miscellaneous

Phage T4 deficient in the enzymes are extremely sensitive to UV.

Catalytic activityi

Cleaves the N-glycosidic bond between the 5'-pyrimidine residue in cyclobutadipyrimidine (in DNA) and the corresponding deoxy-D-ribose residue.2 Publications
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.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei2Nucleophile; via amide nitrogenCombined sources1 Publication1
Sitei3Substrate binding2 Publications1
Sitei22Substrate binding1 Publication1
Active sitei23Proton acceptorCombined sources1 Publication1
Sitei26Transition state stabilizerCombined sources1
Sitei117Substrate binding1 Publication1
Sitei121Substrate binding1 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionEndonuclease, Glycosidase, Hydrolase, Lyase, Multifunctional enzyme, Nuclease
Biological processDNA damage, DNA repair

Enzyme and pathway databases

BRENDAi3.1.25.1 732

Names & Taxonomyi

Protein namesi
Recommended name:
Endonuclease V1 Publication (EC:3.2.2.172 Publications)
Alternative name(s):
DNA-(apurinic or apyrimidinic site) lyase (EC:4.2.99.182 Publications)
Short name:
AP lyase
T4 pyrimidine dimer glycosylase1 Publication
Short name:
T4-Pdg1 Publication
OrganismiEnterobacteria phage T4 (Bacteriophage T4)
Taxonomic identifieri10665 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaeTevenvirinaeT4virus
Virus hostiEscherichia coli [TaxID: 562]
Proteomesi
  • UP000009087 Componenti: Genome
  • UP000001092 Componenti: Genome
  • UP000185270 Componenti: Genome
  • UP000185269 Componenti: Genome
  • UP000185271 Componenti: Genome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi3R → K: Complete loss of DNA glycosylase activity. 1 Publication1
Mutagenesisi11E → Q: 24% decrease in DNA glycosylase activity. 1 Publication1
Mutagenesisi16H → A: 30% decrease in enzymatic activity. 1 Publication1
Mutagenesisi16H → C: 40% decrease in enzymatic activity. 1 Publication1
Mutagenesisi16H → D: 60% decrease in enzymatic activity. 1 Publication1
Mutagenesisi16H → E: 50% decrease in enzymatic activity. 1 Publication1
Mutagenesisi16H → K: 75% decrease in enzymatic activity. 1 Publication1
Mutagenesisi16H → Q: 60% decrease in enzymatic activity. 1 Publication1
Mutagenesisi16H → S: 70% decrease in enzymatic activity. 1 Publication1
Mutagenesisi21Y → F: No effect on DNA glycosylase activity. 1 Publication1
Mutagenesisi22R → Q: Almost complete loss of DNA glycosylase activity. 1 Publication1
Mutagenesisi23E → D: Complete loss of DNA glycosylase activity. No effect on AP lyase activity. 2 Publications1
Mutagenesisi23E → Q: Complete loss of DNA glycosylase activity. Complete loss of AP lyase activity. 2 Publications1
Mutagenesisi26R → Q: Almost complete loss of DNA glycosylase activity. 1 Publication1
Mutagenesisi32R → Q: 10% decrease in DNA glycosylase activity. 1 Publication1
Mutagenesisi40R → Q: 20% decrease in DNA glycosylase activity. 1 Publication1
Mutagenesisi42R → Q: 25% decrease in DNA glycosylase activity. 1 Publication1
Mutagenesisi68R → Q: 35% decrease in DNA glycosylase activity. 1 Publication1
Mutagenesisi86K → Q: No effect on DNA glycosylase activity. 1 Publication1
Mutagenesisi87D → E: No effect on DNA glycosylase activity. 1 Publication1
Mutagenesisi87D → N: 20% decrease in DNA glycosylase activity. 1 Publication1
Mutagenesisi117R → Q: 60% decrease in DNA glycosylase activity. 1 Publication1
Mutagenesisi119D → N: 5% decrease in DNA glycosylase activity. 1 Publication1
Mutagenesisi120E → Q: 10% decrease in DNA glycosylase activity. 1 Publication1
Mutagenesisi121K → Q: 90% decrease in DNA glycosylase activity. 1 Publication1
Mutagenesisi125R → Q: 10% decrease in DNA glycosylase activity. 1 Publication1
Mutagenesisi129Y → F: 65% decrease in DNA glycosylase activity. 1 Publication1
Mutagenesisi132Y → W: 10% decrease in DNA glycosylase activity. 1 Publication1
Mutagenesisi134K → Q: 20% decrease in DNA glycosylase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001649341 – 138Endonuclease VAdd BLAST138

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1138
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 11Combined sources3
Helixi14 – 23Combined sources10
Helixi26 – 36Combined sources11
Helixi41 – 43Combined sources3
Turni54 – 57Combined sources4
Helixi58 – 60Combined sources3
Helixi64 – 80Combined sources17
Helixi98 – 100Combined sources3
Helixi108 – 124Combined sources17
Helixi126 – 128Combined sources3
Beta strandi131 – 133Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ENIX-ray2.20A1-138[»]
1ENJX-ray1.80A1-138[»]
1ENKX-ray2.00A1-138[»]
1VASX-ray2.75A2-138[»]
2ENDX-ray1.45A1-138[»]
2FCCX-ray2.30A/B2-138[»]
ProteinModelPortaliP04418
SMRiP04418
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04418

Family & Domainsi

Phylogenomic databases

KOiK21522
OrthoDBiVOG09000111

Family and domain databases

Gene3Di1.10.440.10, 1 hit
InterProiView protein in InterPro
IPR004260 Pyr-dimer_DNA_glycosylase
IPR021143 Pyr-dimer_DNAGlyclase_EndonucV
IPR024796 T4_endonuc_V
PfamiView protein in Pfam
PF03013 Pyr_excise, 1 hit
PIRSFiPIRSF001000 PDG_ENDV, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD021350 Pyr-dimer_DNA_glycosylase, 1 hit

Sequencei

Sequence statusi: Complete.

P04418-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRINLTLVS ELADQHLMAE YRELPRVFGA VRKHVANGKR VRDFKISPTF
60 70 80 90 100
ILGAGHVTFF YDKLEFLRKR QIELIAECLK RGFNIKDTTV QDISDIPQEF
110 120 130
RGDYIPHEAS IAISQARLDE KIAQRPTWYK YYGKAIYA
Length:138
Mass (Da):16,079
Last modified:August 13, 1987 - v1
Checksum:i90B889C8E6686697
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04567 Genomic DNA Translation: CAA28215.1
AF158101 Genomic DNA Translation: AAD42563.1
HM137666 Genomic DNA Translation: ADJ39840.1
KJ477684 Genomic DNA Translation: AHY83587.1
KJ477685 Genomic DNA Translation: AHY83780.1
KJ477686 Genomic DNA Translation: AHY83971.1
PIRiA93540 NEBPT4
RefSeqiNP_049733.1, NC_000866.4

Genome annotation databases

GeneIDi1258606
KEGGivg:1258606

Similar proteinsi

Entry informationi

Entry nameiEND5_BPT4
AccessioniPrimary (citable) accession number: P04418
Secondary accession number(s): D9IEF4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: May 23, 2018
This is version 116 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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