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O59580 (NTPA_PYRHO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 72. 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:
Non-canonical purine NTP pyrophosphatase
EC=3.6.1.19
Alternative name(s):
Non-standard purine NTP pyrophosphatase
Nucleoside-triphosphate diphosphatase
Nucleoside-triphosphate pyrophosphatase
Short name=NTPase
Gene names
Ordered Locus Names:PH1917
OrganismPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]
Taxonomic identifier70601 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length186 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP/dITP to their respective monophosphate derivatives. Might exclude non-canonical purines from DNA precursor pool, thus preventing their incorporation into DNA and avoiding chromosomal lesions Probable. Ref.2

Catalytic activity

A nucleoside triphosphate + H2O = a nucleotide + diphosphate. HAMAP MF_01405

Cofactor

Binds 1 divalent metal cation ion per subunit; can use either magnesium or manganese Probable. Ref.2

Subunit structure

Homodimer. Ref.2

Sequence similarities

Belongs to the HAM1 NTPase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 186186Non-canonical purine NTP pyrophosphatase HAMAP MF_01405
PRO_0000410428

Regions

Region7 – 126Substrate binding HAMAP MF_01405
Region65 – 662Substrate binding HAMAP MF_01405

Sites

Metal binding361Magnesium or manganese
Metal binding651Magnesium or manganese
Binding site1431Substrate
Binding site1631Substrate
Binding site1691Substrate

Secondary structure

1 ............................... 186
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O59580 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 64FD0922B5C74450

FASTA18621,205
        10         20         30         40         50         60 
MKIFFITSNP GKVREVANFL GTFGIEIVQL KHEYPEIQAE KLEDVVDFGI SWLKGKVPEP 

        70         80         90        100        110        120 
FMIEDSGLFI ESLKGFPGVY SSYVYRTIGL EGILKLMEGA EDRRAYFKSV IGFYIDGKAY 

       130        140        150        160        170        180 
KFSGVTWGRI SNEKRGTHGF GYDPIFIPEG SEKTFAEMTI EEKNALSHRG KALKAFFEWL 


KVNLKY

« Hide

References

« Hide 'large scale' references
[1]"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3."
Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. expand/collapse author list , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.
DNA Res. 5:55-76(1998) [PubMed: 9679194] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
[2]"Structures of dimeric nonstandard nucleotide triphosphate pyrophosphatase from Pyrococcus horikoshii OT3: functional significance of interprotomer conformational changes."
Lokanath N.K., Pampa K.J., Takio K., Kunishima N.
J. Mol. Biol. 375:1013-1025(2008) [PubMed: 18062990] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH ITP; IMP AND MN(2+), FUNCTION, COFACTOR, SUBUNIT.
Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
[3]"Structure of nucleotide triphosphate pyrophosphatase from Pyrococcus horikoshii OT3."
RIKEN structural genomics initiative (RSGI)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ITP.
Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000001 Genomic DNA. Translation: BAA31042.1.
PIRC71206.
RefSeqNP_143746.1. NC_000961.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1V7RX-ray1.40A1-186[»]
2DVNX-ray1.60A/B1-186[»]
2DVOX-ray2.21A1-186[»]
2DVPX-ray1.90A1-186[»]
2E5XX-ray2.00A1-186[»]
2ZTIX-ray2.60A1-186[»]
ProteinModelPortalO59580.
SMRO59580. Positions 1-186.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBPYRT00000000060; EBPYRP00000000060; EBPYRG00000000060.
GeneID1442764.
GenomeReviewsGene locus PH1917 in contig BA000001_GR.
KEGGpho:PH1917.
NMPDRfig|70601.1.peg.1878.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000022850.
HOGENOMHBG697237.
OMAGPYAEYV.
PhylomeDBO59580.
ProtClustDBPRK14821.

Enzyme and pathway databases

BioCycPHOR70601:PH1917-MONOMER.

Family and domain databases

HAMAPMF_01405. Non_canon_purine_NTPase.
[Tree]
InterProIPR002637. Ham1p-like.
IPR020922. Nucleoside-triphosphatase.
[Graphical view]
KOK02428.
PANTHERPTHR11067. Ham1p_like. 1 hit.
PfamPF01725. Ham1p_like. 1 hit.
[Graphical view]
TIGRFAMsTIGR00042. TIGR00042. 1 hit.
ProtoNetSearch...

Entry information

Entry nameNTPA_PYRHO
AccessionPrimary (citable) accession number: O59580
Entry history
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: August 1, 1998
Last modified: January 25, 2012
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents