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Q9R5V5 (NTD_LACLE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nucleoside deoxyribosyltransferase

Short name=N-deoxyribosyltransferase
EC=2.4.2.6
Gene names
Name:ntd
OrganismLactobacillus leichmannii
Taxonomic identifier28039 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length157 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the cleavage of the glycosidic bond of 2'-deoxyribonucleosides and the transfer of the deoxyribosyl moiety to an acceptor purine or pyrimidine base. Ref.1 Ref.2

Catalytic activity

2-deoxy-D-ribosyl-base1 + base2 = 2-deoxy-D-ribosyl-base2 + base1. Ref.1

Pathway

Nucleotide metabolism; nucleotide salvage pathway. Ref.1 Ref.2

Subunit structure

Homohexamer. Ref.2

Sequence similarities

Belongs to the nucleoside deoxyribosyltransferase family.

Caution

Was originally (Ref.1) thought to originate from E.coli.

Biophysicochemical properties

pH dependence:

Optimum pH is 6.0.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 157156Nucleoside deoxyribosyltransferase
PRO_0000220067

Sites

Active site981Nucleophile Ref.1

Experimental info

Mutagenesis981E → A: Loss of transferase activity. Ref.1

Secondary structure

................................. 157
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9R5V5 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: F3CA8CA6F509A91F

FASTA15718,080
        10         20         30         40         50         60 
MPKKTIYFGA GWFTDRQNKA YKEAMEALKE NPTIDLENSY VPLDNQYKGI RVDEHPEYLH 

        70         80         90        100        110        120 
DKVWATATYN NDLNGIKTND IMLGVYIPDE EDVGLGMELG YALSQGKYVL LVIPDEDYGK 

       130        140        150 
PINLMSWGVS DNVIKMSQLK DFNFNKPRFD FYEGAVY 

« Hide

References

[1]"Identification of the active site nucleophile in nucleoside 2-deoxyribosyltransferase as glutamic acid 98."
Porter D.J.T., Merrill B.M., Short S.A.
J. Biol. Chem. 270:15551-15556(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-26, FUNCTION, ACTIVE SITE, MUTAGENESIS OF GLU-98.
[2]"Crystal structures of nucleoside 2-deoxyribosyltransferase in native and ligand-bound forms reveal architecture of the active site."
Armstrong S.R., Cook W.J., Short S.A., Ealick S.E.
Structure 4:97-107(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F8XX-ray2.50A/B1-157[»]
1F8YX-ray2.40A/B1-157[»]
4HX9X-ray2.68A/B/C/D/E/F/G/H1-157[»]
ProteinModelPortalQ9R5V5.
SMRQ9R5V5. Positions 2-157.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00312.

Family and domain databases

Gene3D3.40.50.1810. 1 hit.
InterProIPR007710. Nucleoside_deoxyribTrfase.
[Graphical view]
PfamPF05014. Nuc_deoxyrib_tr. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9R5V5.

Entry information

Entry nameNTD_LACLE
AccessionPrimary (citable) accession number: Q9R5V5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 53 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways