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P80562 (IPYR_NOSS1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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:all3570
OrganismNostoc sp. (strain PCC 7120 / UTEX 2576) [Complete proteome] [HAMAP]
Taxonomic identifier103690 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeNostoc

Protein attributes

Sequence length169 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes PPi generated in anabolic reactions. HAMAP MF_00209

Catalytic activity

Diphosphate + H2O = 2 phosphate. Ref.1

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. In the presence of zinc, manganese, copper, iron or cobalt ions, activity is very low. In the absence of metal ions, there is no activity. Ref.1

Subunit structure

Homohexamer. Ref.1

Subcellular location

Cytoplasm HAMAP MF_00209.

Sequence similarities

Belongs to the PPase family.

Biophysicochemical properties

Kinetic parameters:

KM=3 µM for PPi Ref.1

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   PTMFormylation
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processphosphate-containing compound 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: EC

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 169169Inorganic pyrophosphatase HAMAP MF_00209
PRO_0000137474

Sites

Metal binding641Magnesium 1 By similarity
Metal binding691Magnesium 1 By similarity
Metal binding691Magnesium 2 By similarity
Metal binding1011Magnesium 1 By similarity

Amino acid modifications

Modified residue11N-formylmethionine HAMAP MF_00209

Experimental info

Sequence conflict1171V → R in CAC81009. Ref.1
Sequence conflict148 – 1492IL → SV in CAC81009. Ref.1
Sequence conflict163 – 1653QSI → HPV in CAC81009. Ref.1
Sequence conflict1691K → T in CAC81009. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P80562 [UniParc].

Last modified February 11, 2002. Version 1.
Checksum: 17A027E16C2289D3

FASTA16918,961
        10         20         30         40         50         60 
MDLSRIPAQP KPGVINILIE IAGGSQNKYE FDKDLEAFAL DRVLYSSVKY PYDYGFVPNT 

        70         80         90        100        110        120 
LADDGDPLDG MVIIDEPTFP GCVIAARPIG FLEMIDGGDR DEKILAVPDK DPRYAHVKSL 

       130        140        150        160 
NDVAPHRLDE IAEFFRSYKN LEKKVTQILG WQDVDQVKAL VDQSIKAYK 

« Hide

References

« Hide 'large scale' references
[1]"Comparative biochemical and functional studies of family I soluble inorganic pyrophosphatases from photosynthetic bacteria."
Gomez-Garcia M.R., Losada M., Serrano A.
FEBS J. 274:3948-3959(2007) [PubMed: 17635582] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-23, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, FORMYLATION AT MET-1.
[2]"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120."
Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takazawa M., Yamada M., Yasuda M., Tabata S.
DNA Res. 8:205-213(2001) [PubMed: 11759840] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7120 / UTEX 2576.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ252206 Genomic DNA. Translation: CAC81009.2.
BA000019 Genomic DNA. Translation: BAB75269.1.
PIRAC2252.
RefSeqNP_487610.1. NC_003272.1.

3D structure databases

ProteinModelPortalP80562.
ModBaseSearch...

Protein-protein interaction databases

STRINGP80562.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1107168.
GenomeReviewsGene locus all3570 in contig BA000019_GR.
KEGGana:all3570.
NMPDRfig|103690.1.peg.3877.
PATRIC22777570. VBINosSp37423_4240.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0221.
HOGENOMHBG529150.
OMAPNDFNVI.
PhylomeDBP80562.
ProtClustDBCLSK895996.

Enzyme and pathway databases

BioCycNSP103690:ALL3570-MONOMER.

Family and domain databases

HAMAPMF_00209. Inorganic_PPase.
[Tree]
InterProIPR008162. Pyrophosphatase.
[Graphical view]
Gene3DG3DSA:3.90.80.10. Pyrophosphatase. 1 hit.
KOK01507.
PANTHERPTHR10286. Pyrophosphatase. 1 hit.
PfamPF00719. Pyrophosphatase. 1 hit.
[Graphical view]
SUPFAMSSF50324. Pyrophosphatase. 1 hit.
PROSITEPS00387. PPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIPYR_NOSS1
AccessionPrimary (citable) accession number: P80562
Secondary accession number(s): Q8YR78
Entry history
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: February 11, 2002
Last modified: January 25, 2012
This is version 62 of the entry and version 1 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