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Reviewed, UniProtKB/Swiss-Prot P38576 (IPYR_THET8)

Last modified November 3, 2009. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
    Inorganic pyrophosphatase
    EC=3.6.1.1
Alternative name(s):
    Pyrophosphate phospho-hydrolase
      Short name=PPase
Gene names
Name: ppa
Ordered Locus Names: TTHA1965
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Complete proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length175 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

Diphosphate + H2O = 2 phosphate. HAMAP MF_00209

Cofactor

Binds 4 magnesium ions per subunit. Other metal ions can support activity, but at a lower rate. Two magnesium ions are required for the activation of the enzyme and are present before substrate binds, two additional magnesium ions form complexes with substrate and product. HAMAP MF_00209

Subunit structure

Homohexamer. HAMAP MF_00209

Subcellular location

Cytoplasm. HAMAP MF_00209

Sequence similarities

Belongs to the PPase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processphosphate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioninorganic diphosphatase activity

Inferred from electronic annotation. Source: HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed HAMAP MF_00209
Chain2 – 175174Inorganic pyrophosphatase HAMAP MF_00209
PRO_0000137535

Sites

Metal binding661Magnesium 1 HAMAP MF_00209
Metal binding711Magnesium 1 HAMAP MF_00209
Metal binding711Magnesium 2 HAMAP MF_00209
Metal binding1031Magnesium 1 HAMAP MF_00209

Secondary structure

................................ 175
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P38576-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 01306D30B31DB061

FASTA17519,216
        10         20         30         40         50         60 
MANLKSLPVG DKAPEVVHMV IEVPRGSGNK YEYDPDLGAI KLDRVLPGAQ FYPGDYGFIP 

        70         80         90        100        110        120 
STLAEDGDPL DGLVLSTYPL LPGVVVEVRV VGLLLMEDEK GGDAKVIGVV AEDQRLDHIQ 

       130        140        150        160        170 
DIGDVPEGVK QEIQHFFETY KALEAKKGKW VKVTGWRDRK AALEEVRACI ARYKG 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning, expression, and site-directed mutagenesis of inorganic pyrophosphatase from Thermus thermophilus HB8."
Satoh T., Samejima T., Watanabe M., Nogi S., Takahashi Y., Kaji H., Teplyakov A., Obmolova G., Kuranova I., Ishii K.
J. Biochem. 124:79-88(1998) [PubMed: 9644249] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]"Complete genome sequence of Thermus thermophilus HB8."
Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Crystal structure of inorganic pyrophosphatase from Thermus thermophilus."
Teplyakov A., Obmolova G., Wilson K.S., Ishii K., Kaji H., Samejima T., Kuranova I.
Protein Sci. 3:1098-1107(1994) [PubMed: 7920256] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

AB010580 Genomic DNA. Translation: BAA24521.1.
AP008226 Genomic DNA. Translation: BAD71788.1.
RefSeqYP_145231.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2PRDX-ray2.00A2-175[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGP38576.

Genome annotation databases

GeneID3169724.
GenomeReviewsGene locus TTHA1965 in contig AP008226_GR.
KEGGttj:TTHA1965.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP38576.
OMAEIDKDTG.

Enzyme and pathway databases

BioCycTTHE300852:TTHA1965-MON.

Family and domain databases

HAMAPMF_00209.
[Tree]
InterProIPR008162. Pyrophosphatase.
[Graphical view]
Gene3DG3DSA:3.90.80.10. Pyrophosphatase. 1 hit.
PANTHERPTHR10286. Pyrophosphatase. 1 hit.
PfamPF00719. Pyrophosphatase. 1 hit.
[Graphical view]
ProDomPD002014. Inorg_pphsph. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00387. PPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIPYR_THET8
AccessionPrimary (citable) accession number: P38576
Secondary accession number(s): Q5SGW5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: January 23, 2007
Last modified: November 3, 2009
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

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