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Protein

Pyrophosphatase PpaX

Gene

ppaX

Organism
Bacillus cereus (strain AH187)
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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei9 – 91NucleophileUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium

Enzyme and pathway databases

BioCyciBCER405534:GHXM-5247-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyrophosphatase PpaXUniRule annotation (EC:3.6.1.1UniRule annotation)
Gene namesi
Name:ppaXUniRule annotation
Ordered Locus Names:BCAH187_A5322
OrganismiBacillus cereus (strain AH187)
Taxonomic identifieri405534 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000002214 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 216216Pyrophosphatase PpaXPRO_1000139926Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliB7HWY7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000248344.
KOiK06019.
OMAiYEPDFML.
OrthoDBiEOG6K404V.

Family and domain databases

Gene3Di1.10.150.240. 1 hit.
3.40.50.1000. 1 hit.
HAMAPiMF_01250. Pyrophosphat_PpaX.
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.

B7HWY7-1 [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:February 10, 2009 - v1
Checksum:iE0285BB4D9B2BB4E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001177 Genomic DNA. Translation: ACJ80542.1.
RefSeqiWP_000700963.1. NC_011658.1.

Genome annotation databases

EnsemblBacteriaiACJ80542; ACJ80542; BCAH187_A5322.
KEGGibcr:BCAH187_A5322.
PATRICi18836067. VBIBacCer120511_5476.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001177 Genomic DNA. Translation: ACJ80542.1.
RefSeqiWP_000700963.1. NC_011658.1.

3D structure databases

ProteinModelPortaliB7HWY7.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACJ80542; ACJ80542; BCAH187_A5322.
KEGGibcr:BCAH187_A5322.
PATRICi18836067. VBIBacCer120511_5476.

Phylogenomic databases

HOGENOMiHOG000248344.
KOiK06019.
OMAiYEPDFML.
OrthoDBiEOG6K404V.

Enzyme and pathway databases

BioCyciBCER405534:GHXM-5247-MONOMER.

Family and domain databases

Gene3Di1.10.150.240. 1 hit.
3.40.50.1000. 1 hit.
HAMAPiMF_01250. Pyrophosphat_PpaX.
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...

Publicationsi

  1. "Genome sequence of Bacillus cereus AH187."
    Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B., Okstad O.A., Ravel J., Sutton G.
    Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AH187.

Entry informationi

Entry nameiPPAX_BACC7
AccessioniPrimary (citable) accession number: B7HWY7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: July 6, 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.