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Reviewed, UniProtKB/Swiss-Prot P19514 (IPYR_BACP3)

Last modified June 16, 2009. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismBacillus PS3 (Thermophilic bacterium PS-3)
Taxonomic identifier2334 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length165 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 By similarity.

Subunit structure

Homotrimer. In presence of divalent cations the trimers aggregate to form a hexamer. 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 termDirect 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 Ref.1
Chain2 – 165164Inorganic pyrophosphatase HAMAP MF_00209
PRO_0000137478

Sites

Metal binding571Magnesium 1 By similarity
Metal binding621Magnesium 1 By similarity
Metal binding621Magnesium 2 By similarity
Metal binding941Magnesium 1 By similarity

Sequences

Sequence LengthMass (Da)Tools
P19514-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 38BD173CE5622C2F

FASTA16518,923
        10         20         30         40         50         60 
MAFENKIVEA FIEIPTGSQN KYEFDKERGI FKLDRVLYSP MFYPAEYGYL QNTLALDGDP 

        70         80         90        100        110        120 
LDILVITTNP PFPGCVIDTR VIGYLNMVDS GEEDAKLIGV PVEDPRFDEV RSIEDLPQHK 

       130        140        150        160 
LKEIAHFFER YKDLQGKRTE IGTWEGPEAA AKLIDECIAR YNEQK 

« Hide

References

[1]"Primary structure of the inorganic pyrophosphatase from thermophilic bacterium PS-3."
Ichiba T., Takenaka O., Samejima T., Hachimori A.
J. Biochem. 108:572-578(1990) [PubMed: 1963432] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-165.

Cross-references

Sequence databases

PIRJX0135.

3D structure databases

HSSPHSSP built from PDB template 1FAJ based on UniProtKB P17288.
ModBaseSearch...

Enzyme and pathway databases

BRENDA3.6.1.1. 276726.

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_BACP3
AccessionPrimary (citable) accession number: P19514
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 59 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

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