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Q5PJ75 (Q5PJ75_SALPA) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Inorganic pyrophosphatase HAMAP-Rule MF_00209

EC=3.6.1.1 HAMAP-Rule MF_00209
Alternative name(s):
Pyrophosphate phospho-hydrolase HAMAP-Rule MF_00209
Gene names
Name:ppa HAMAP-Rule MF_00209 EMBL AAV79970.1
Ordered Locus Names:SPA4234 EMBL AAV79970.1
OrganismSalmonella paratyphi A (strain ATCC 9150 / SARB42) [Complete proteome] [HAMAP] EMBL AAV79970.1
Taxonomic identifier295319 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length176 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Diphosphate + H2O = 2 phosphate. HAMAP-Rule 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. HAMAP-Rule MF_00209

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00209.

Sequence similarities

Belongs to the PPase family. HAMAP-Rule MF_00209

Ontologies

Keywords
   Cellular componentCytoplasm HAMAP-Rule MF_00209
   LigandMagnesium HAMAP-Rule MF_00209
Metal-binding HAMAP-Rule MF_00209
   Molecular functionHydrolase HAMAP-Rule MF_00209
   Technical termComplete proteome
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: UniProtKB-HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Metal binding661Magnesium 1 By similarity HAMAP-Rule MF_00209
Metal binding711Magnesium 1 By similarity HAMAP-Rule MF_00209
Metal binding711Magnesium 2 By similarity HAMAP-Rule MF_00209
Metal binding1031Magnesium 1 By similarity HAMAP-Rule MF_00209

Sequences

Sequence LengthMass (Da)Tools
Q5PJ75 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 3C00EC5AA02B1BB2

FASTA17619,677
        10         20         30         40         50         60 
MSLLNVPAGK ELPEDIYVVI EIPANADPIK YEVDKESGAL FVDRFMSTAM FYPCNYGYIN 

        70         80         90        100        110        120 
HTLSLDGDPV DVLVPTPYPL QPGAVIRCRP VGVLKMTDES GEDAKLVAVP HTKLSKEYDH 

       130        140        150        160        170 
IKDVNDLPEL LKAQITHFFE HYKDLEKGKW VKVDGWDNAE AAKAEIVASF ERAAKK 

« Hide

References

[1]"Comparison of genome degradation in Paratyphi A and Typhi, human-restricted serovars of Salmonella enterica that cause typhoid."
McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F. expand/collapse author list , Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W., Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M., Warren W., Florea L., Spieth J., Wilson R.K.
Nat. Genet. 36:1268-1274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 9150 / SARB42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000026 Genomic DNA. Translation: AAV79970.1.
RefSeqYP_153282.1. NC_006511.1.

3D structure databases

ProteinModelPortalQ5PJ75.
SMRQ5PJ75. Positions 2-176.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING295319.SPA4234.

Proteomic databases

PRIDEQ5PJ75.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV79970; AAV79970; SPA4234.
PATRIC32358279. VBISalEnt134188_4486.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000236473.
OMAVEAIYIR.
OrthoDBEOG6NKR4X.

Enzyme and pathway databases

BioCycSENT295319:GJBZ-4228-MONOMER.

Family and domain databases

Gene3D3.90.80.10. 1 hit.
HAMAPMF_00209. Inorganic_PPase.
InterProIPR008162. Pyrophosphatase.
[Graphical view]
PANTHERPTHR10286. PTHR10286. 1 hit.
PfamPF00719. Pyrophosphatase. 1 hit.
[Graphical view]
SUPFAMSSF50324. SSF50324. 1 hit.
PROSITEPS00387. PPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ5PJ75_SALPA
AccessionPrimary (citable) accession number: Q5PJ75
Entry history
Integrated into UniProtKB/TrEMBL: January 4, 2005
Last sequence update: January 4, 2005
Last modified: June 11, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)