P50308 (IPYR_SULAC) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 79.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Inorganic pyrophosphatase EC=3.6.1.1 Alternative name(s): Pyrophosphate phospho-hydrolase Short name=PPase | ||||
| Gene names |
| ||||
| Organism | Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 330779 [NCBI] | ||||
| Taxonomic lineage | Archaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Sulfolobus |
Protein attributes
| Sequence length | 173 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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 that are present before substrate binds, two additional magnesium ions form complexes with substrate and product. |
| Subunit structure | Homohexamer. |
| Subcellular location | |
| Sequence similarities | Belongs to the PPase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | Magnesium Metal-binding |
| Molecular function | Hydrolase |
| Technical term | 3D-structure Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | phosphate-containing compound metabolic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | inorganic diphosphatase activity Inferred from electronic annotation. Source: EC magnesium ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 173 | 173 | Inorganic pyrophosphatase HAMAP MF_00209 | PRO_0000137559 | |||||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||||
| Metal binding | 62 | 1 | Magnesium 1 | ||||||||||||||||||||||||||||||||||||
| Metal binding | 67 | 1 | Magnesium 2 | ||||||||||||||||||||||||||||||||||||
| Metal binding | 99 | 1 | Magnesium 1 | ||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||
| Turn | 7 – 11 | 5 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 12 – 19 | 8 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 25 – 30 | 6 | |||||||||||||||||||||||||||||||||||||
| Turn | 31 – 34 | 4 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 35 – 41 | 7 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 43 – 46 | 4 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 49 – 54 | 6 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 67 – 70 | 4 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 81 – 94 | 14 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 97 – 106 | 10 | |||||||||||||||||||||||||||||||||||||
| Turn | 108 – 110 | 3 | |||||||||||||||||||||||||||||||||||||
| Helix | 112 – 114 | 3 | |||||||||||||||||||||||||||||||||||||
| Helix | 120 – 122 | 3 | |||||||||||||||||||||||||||||||||||||
| Helix | 125 – 137 | 13 | |||||||||||||||||||||||||||||||||||||
| Turn | 138 – 141 | 4 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 147 – 153 | 7 | |||||||||||||||||||||||||||||||||||||
| Helix | 155 – 169 | 15 | |||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Purification, cloning, and sequencing of archaebacterial pyrophosphatase from the extreme thermoacidophile Sulfolobus acidocaldarius." Meyer W., Moll R., Kath T., Schaefer G. Arch. Biochem. Biophys. 319:149-156(1995) [PubMed: 7771779] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION. Strain: ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770. |
| [2] | "The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota." Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E., Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A. J. Bacteriol. 187:4992-4999(2005) [PubMed: 15995215] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770. |
| [3] | "Sulfolobus acidocaldarius inorganic pyrophosphatase: structure, thermostability, and effect of metal ion in an archael pyrophosphatase." Leppaenen V.-M., Nummelin H., Hansen T., Lahti R., Schaefer G., Goldman A. Protein Sci. 8:1218-1231(1999) [PubMed: 10386872] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS). Strain: ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | X81842 Genomic DNA. Translation: CAA57434.1. CP000077 Genomic DNA. Translation: AAY80317.1. | ||||||||||||
| PIR | S57617. S65965. | ||||||||||||
| RefSeq | YP_255610.1. NC_007181.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P50308. | ||||||||||||
| SMR | P50308. Positions 2-170. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 3472897. | ||||||||||||
| GenomeReviews | Gene locus Saci_0955 in contig CP000077_GR. | ||||||||||||
| KEGG | sai:Saci_0955. | ||||||||||||
| NMPDR | fig|330779.3.peg.1112. | ||||||||||||
Organism-specific databases | |||||||||||||
| CMR | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | HBG529150. | ||||||||||||
| OMA | PNDFNVI. | ||||||||||||
| PhylomeDB | P50308. | ||||||||||||
| ProtClustDB | PRK01250. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | SACI330779:SACI_0955-MONOMER. | ||||||||||||
Family and domain databases | |||||||||||||
| HAMAP | MF_00209. Inorganic_PPase. [Tree] | ||||||||||||
| InterPro | IPR008162. Pyrophosphatase. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:3.90.80.10. Pyrophosphatase. 1 hit. | ||||||||||||
| KO | K01507. | ||||||||||||
| PANTHER | PTHR10286. Pyrophosphatase. 1 hit. | ||||||||||||
| Pfam | PF00719. Pyrophosphatase. 1 hit. [Graphical view] | ||||||||||||
| SUPFAM | SSF50324. Pyrophosphatase. 1 hit. | ||||||||||||
| PROSITE | PS00387. PPASE. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | IPYR_SULAC | ||||||||
| Accession | Primary (citable) accession number: P50308 Secondary accession number(s): Q4JA63 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with