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Protein

Pyrophosphatase PpaX

Gene

ppaX

Organism
Bacillus cereus (strain Q1)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Hydrolyzes pyrophosphate formed during P-Ser-HPr dephosphorylation by HPrK/P. Might play a role in controlling the intracellular pyrophosphate pool.UniRule annotation

Catalytic activityi

Diphosphate + H2O = 2 phosphate.UniRule annotation

Cofactori

Mg2+UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei9NucleophileUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium

Names & Taxonomyi

Protein namesi
Recommended name:
Pyrophosphatase PpaXUniRule annotation (EC:3.6.1.1UniRule annotation)
Gene namesi
Name:ppaXUniRule annotation
Ordered Locus Names:BCQ_4982
OrganismiBacillus cereus (strain Q1)
Taxonomic identifieri361100 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000000441 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001650851 – 216Pyrophosphatase PpaXAdd BLAST216

Structurei

3D structure databases

ProteinModelPortaliB9J4R5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the HAD-like hydrolase superfamily. PpaX family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000248344.
KOiK06019.
OMAiYEPDFML.

Family and domain databases

Gene3Di1.10.150.240. 1 hit.
3.40.50.1000. 1 hit.
HAMAPiMF_01250. Pyrophosphat_PpaX. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
IPR006549. HAD-SF_hydro_IIIA.
IPR023198. PGP_dom2.
IPR023733. Pyrophosphatase_Ppax.
[Graphical view]
PfamiPF13419. HAD_2. 1 hit.
[Graphical view]
PRINTSiPR00413. HADHALOGNASE.
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01549. HAD-SF-IA-v1. 1 hit.
TIGR01509. HAD-SF-IA-v3. 1 hit.
TIGR01662. HAD-SF-IIIA. 1 hit.

Sequencei

Sequence statusi: Complete.

B9J4R5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKINTVLFDL DGTLINTNEL IISSFLHTLN TYYPDQYKRE DVLPFIGPSL
60 70 80 90 100
HDTFSKIDES KVEELITSYR QFNHDHHDEL VEEYETVYET VQELKKQGYK
110 120 130 140 150
VGIVTTKARQ TVEMGLKLSK LDEFFDVVVT IDDVEHVKPH PEPLQKALQL
160 170 180 190 200
LDAKPEEALM VGDNHHDIVG GQNAGTKTAA VSWTLKGRAY LEAYKPDFML
210
DKMSDLLPIL SDMNRS
Length:216
Mass (Da):24,699
Last modified:March 24, 2009 - v1
Checksum:iE0285BB4D9B2BB4E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000227 Genomic DNA. Translation: ACM15382.1.
RefSeqiWP_000700963.1. NC_011969.1.

Genome annotation databases

EnsemblBacteriaiACM15382; ACM15382; BCQ_4982.
KEGGibcq:BCQ_4982.
PATRICi18917777. VBIBacCer120424_5027.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000227 Genomic DNA. Translation: ACM15382.1.
RefSeqiWP_000700963.1. NC_011969.1.

3D structure databases

ProteinModelPortaliB9J4R5.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACM15382; ACM15382; BCQ_4982.
KEGGibcq:BCQ_4982.
PATRICi18917777. VBIBacCer120424_5027.

Phylogenomic databases

HOGENOMiHOG000248344.
KOiK06019.
OMAiYEPDFML.

Family and domain databases

Gene3Di1.10.150.240. 1 hit.
3.40.50.1000. 1 hit.
HAMAPiMF_01250. Pyrophosphat_PpaX. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
IPR006549. HAD-SF_hydro_IIIA.
IPR023198. PGP_dom2.
IPR023733. Pyrophosphatase_Ppax.
[Graphical view]
PfamiPF13419. HAD_2. 1 hit.
[Graphical view]
PRINTSiPR00413. HADHALOGNASE.
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01549. HAD-SF-IA-v1. 1 hit.
TIGR01509. HAD-SF-IA-v3. 1 hit.
TIGR01662. HAD-SF-IIIA. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPPAX_BACCQ
AccessioniPrimary (citable) accession number: B9J4R5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: November 2, 2016
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.