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Reviewed, UniProtKB/Swiss-Prot P52061 (RDGB_ECOLI)

Last modified June 16, 2009. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Nucleoside-triphosphatase rdgB
    EC=3.6.1.15
Alternative name(s):
    Nucleoside triphosphate phosphohydrolase
      Short name=NTPase
Gene names
Name: rdgB
Synonyms: yggV
Ordered Locus Names: b2954, JW2921
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length197 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Hydrolyzes O6 atom-containing purine bases deoxyinosine triphosphate (dITP) and xanthosine triphosphate (XTP) as well as 2'-deoxy-N-6-hydroxylaminopurine triposphate (dHAPTP) to nucleotide monophosphate and pyrophosphate. Probably excludes non-standard purines from DNA precursor pool, preventing thus incorporation into DNA and avoiding chromosomal lesions. Ref.4

Catalytic activity

NTP + H2O = NDP + phosphate. Ref.3

Cofactor

Divalent cations. Maximum activity is obtained with magnesium. Activity with manganese and nickel makes up 60-75% of the maximum rate. Ref.3

Subunit structure

Homodimer. Ref.3

Miscellaneous

Activity toward dATP, dCTP and dTTP is less than 1% of the rate of XTP hydrolysis. Activity toward dGTP and dUTP is 10-12% lower than activity toward XTP. Modified or damaged nucleotides such as 6-chloropurine deoxyribose triphosphate, 8-Br-dGTP, 5-Br-dCTP, 5-Br-dUTP, 7-deaza-dGTP, 7-methyl-GTP, N6-etheno-ATP, NAD, NADH, FAD, ADP-ribose, UPD-glucose, AppA and ApppA are not hydrolyzed. HAMAP MF_01405

Sequence similarities

Belongs to the HAM1 NTPase family.

biophysicochemical properties

Kinetic parameters:

Vmax values are similar for XTP, dITP and ITP.

KM=0.33 mM for XTP HAMAP MF_01405

KM=0.36 mM for dITP

KM=0.41 mM for ITP

KM=16.5 µM for dHAPTP

pH dependence:

Optimum pH is 10-10.5.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 197197Nucleoside-triphosphatase rdgB HAMAP MF_01405
PRO_0000178164

Secondary structure

.................................... 197
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P52061-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 74E82A59B1A9E294

FASTA19721,039
        10         20         30         40         50         60 
MQKVVLATGN VGKVRELASL LSDFGLDIVA QTDLGVDSAE ETGLTFIENA ILKARHAAKV 

        70         80         90        100        110        120 
TALPAIADDS GLAVDVLGGA PGIYSARYSG EDATDQKNLQ KLLETMKDVP DDQRQARFHC 

       130        140        150        160        170        180 
VLVYLRHAED PTPLVCHGSW PGVITREPAG TGGFGYDPIF FVPSEGKTAA ELTREEKSAI 

       190 
SHRGQALKLL LDALRNG 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[2]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"Identification of the dITP- and XTP-hydrolyzing protein from Escherichia coli."
Chung J.H., Park H.-Y., Lee J.H., Jang Y.
J. Biochem. Mol. Biol. 35:403-408(2002) [PubMed: 12297000] [Abstract]
Cited for: CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
[4]"Substrate specificity of RdgB protein, a deoxyribonucleoside triphosphate pyrophosphohydrolase."
Burgis N.E., Cunningham R.P.
J. Biol. Chem. 282:3531-3538(2007) [PubMed: 17090528] [Abstract]
Cited for: SUBSTRATE SPECIFICITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[5]"Putative ribosomal protein."
Midwest center for structural genomics (MCSG)
Submitted (JAN-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

U28377 Genomic DNA. Translation: AAA69121.1.
U00096 Genomic DNA. Translation: AAC75991.1.
AP009048 Genomic DNA. Translation: BAE77017.1.
PIRA65081.
RefSeqAP_003511.1.
NP_417429.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1K7KX-ray1.50A1-197[»]
2PYUX-ray2.02A1-197[»]
2Q16X-ray1.95A/B1-197[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:12197N.

Genome annotation databases

GeneID947429.
GenomeReviewsGene locus JW2921 in contig AP009048_GR.
Gene locus b2954 in contig U00096_GR.
KEGGecj:JW2921.
eco:b2954.

Organism-specific databases

EchoBASEEB2807.
EcoGeneEG12982. rdgB.
CMRSearch...

Phylogenomic databases

HOGENOMP52061.
OMAP52061. VYTADWA.

Enzyme and pathway databases

BioCycEcoCyc:G7530-MON.
MetaCyc:G7530-MON.

Family and domain databases

HAMAPMF_01405.
[Tree]
InterProIPR002637. Ham1p-like.
[Graphical view]
PANTHERPTHR11067. Ham1p_like. 1 hit.
PfamPF01725. Ham1p_like. 1 hit.
[Graphical view]
TIGRFAMsTIGR00042. Ham1p_like. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRDGB_ECOLI
AccessionPrimary (citable) accession number: P52061
Secondary accession number(s): Q2M9N9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 16, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents