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Q68WP2

- PPDK_RICTY

UniProt

Q68WP2 - PPDK_RICTY

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Protein

Pyruvate, phosphate dikinase

Gene
ppdK, RT0478
Organism
Rickettsia typhi (strain ATCC VR-144 / Wilmington)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

Catalyzes the reversible phosphorylation of pyruvate and phosphate By similarity.

Catalytic activityi

ATP + pyruvate + phosphate = AMP + phosphoenolpyruvate + diphosphate.

Cofactori

Magnesium By similarity.

Enzyme regulationi

Activated by light-induced dephosphorylation. Inhibited by dark-induced phosphorylation. Both reactions are catalyzed by PDRP1 By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei97 – 971ATP Reviewed prediction
Active sitei460 – 4601Tele-phosphohistidine intermediate By similarity
Binding sitei566 – 5661Substrate By similarity
Binding sitei622 – 6221Substrate By similarity
Metal bindingi750 – 7501Magnesium By similarity
Binding sitei750 – 7501Substrate By similarity
Binding sitei771 – 7711Substrate; via carbonyl oxygen By similarity
Binding sitei772 – 7721Substrate; via amide nitrogen By similarity
Binding sitei773 – 7731Substrate By similarity
Metal bindingi774 – 7741Magnesium By similarity
Binding sitei774 – 7741Substrate; via amide nitrogen By similarity
Active sitei836 – 8361Proton donor By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. kinase activity Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW
  4. pyruvate, phosphate dikinase activity Source: UniProtKB-EC

GO - Biological processi

  1. pyruvate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciRTYP257363:GJEQ-501-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate, phosphate dikinase (EC:2.7.9.1)
Alternative name(s):
Pyruvate, orthophosphate dikinase
Gene namesi
Name:ppdK
Ordered Locus Names:RT0478
OrganismiRickettsia typhi (strain ATCC VR-144 / Wilmington)
Taxonomic identifieri257363 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group
ProteomesiUP000000604: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 880880Pyruvate, phosphate dikinasePRO_0000289279Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei458 – 4581Phosphothreonine; by PDRP1 By similarity

Post-translational modificationi

Phosphorylation of Thr-458 in the dark inactivates the enzyme. Dephosphorylation upon light stimulation reactivates the enzyme By similarity.

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Homodimer By similarity.

Protein-protein interaction databases

STRINGi257363.RT0478.

Structurei

3D structure databases

ProteinModelPortaliQ68WP2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 348348N-terminalAdd
BLAST
Regioni349 – 40557Linker 1Add
BLAST
Regioni406 – 50398CentralAdd
BLAST
Regioni504 – 53835Linker 2Add
BLAST
Regioni539 – 879341C-terminalAdd
BLAST

Domaini

The N-terminal domain contains the ATP/Pi active site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate active site By similarity.

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0574.
HOGENOMiHOG000039664.
KOiK01006.
OMAiAVIYRKI.
OrthoDBiEOG6N0HGQ.

Family and domain databases

Gene3Di3.20.20.60. 1 hit.
3.30.1490.20. 2 hits.
3.30.470.20. 1 hit.
3.50.30.10. 1 hit.
InterProiIPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR008279. PEP-util_enz_mobile_dom.
IPR018274. PEP_util_AS.
IPR000121. PEP_util_C.
IPR023151. PEP_util_CS.
IPR002192. PPDK_PEP-bd.
IPR010121. Pyruvate_phosphate_dikinase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PANTHERiPTHR22931:SF9. PTHR22931:SF9. 1 hit.
PfamiPF00391. PEP-utilizers. 1 hit.
PF02896. PEP-utilizers_C. 1 hit.
PF01326. PPDK_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000853. PPDK. 1 hit.
SUPFAMiSSF51621. SSF51621. 1 hit.
SSF52009. SSF52009. 1 hit.
TIGRFAMsiTIGR01828. pyru_phos_dikin. 1 hit.
PROSITEiPS00742. PEP_ENZYMES_2. 1 hit.
PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q68WP2-1 [UniParc]FASTAAdd to Basket

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MNKLIYYFGN NGSDGNASMK NILGNKGAGL AEMSNLKLPI PNGFTITTEL    50
CNYFYKHNNN LPKNFQNELQ QAITKLEITT GKIFGSTTSN PLLLSVRSGS 100
TVSMPGMMDT ILNLGMNNEV CNALADSCGN KLFALDSYRR FLEMYGSTVL 150
SIPSDLFEQI YEKHKVQADI YKDSDITVEL LEKIIDDFKR LHIKYTKQLI 200
KDPYEQLESA IKAVLYSWKN NRAIVYRKLN NISEDFGTAI NIQEMVFGNL 250
GKTSATGVVF TRSPSTGEKK LFGEFLINAQ GEDIVSGTRT PMPIIANDSN 300
SMQAMMPEVF TKLSQIAKKL EEHYLDMQDI EFTIENNKLY ILQTRTAKRT 350
AIAAINIAVQ MVEEKLISKE QALMRIDPES LNQLLHTRID YSKKLTAIAE 400
GLPASPGAAT GIVVFSPYDA EKLSHHHKVI LVRHDTSPED INGMHVASGI 450
LTIRGGMTSH AAVVARGMGK PCVCGTNNLS IDEQKQILIA GDIVIKQGDI 500
ITIDGGSGKI FLGEMPLIQP TFSEESTLIL DWADEISSLK VRANAETVND 550
ALVSIKFGAQ GIGLCRSEHM FFDKNKIPLV REMIIAPDIE RRQCALQKLL 600
PLQTEDFKAL FRVMKNKPVN IRLLDPPLHE FLPTTDEDKK NLAHSLNLPL 650
SMIHQRLHAM HEVNPMLGHR GCRLGICLPE IYQMQIEAIL TAIFELHKKE 700
HIESNLELMI PLISNVAEIK KLKMDIYAVV KKLEQRYSYK FSFTLGTMIE 750
LPRAALGSKK IAKEVDYFSF GTNDLTQTTY GISRDDIASF LPYYLEEKIF 800
ESDPFTTLDE EGVGELIKIA IKRGKSSNAN LKLGACGEHA GNPTSIAFFH 850
KMNLNYVSCS PYRIPIARIA AAQAKIKQGS 880
Length:880
Mass (Da):98,165
Last modified:October 11, 2004 - v1
Checksum:iFFFE55AEEA138B34
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE017197 Genomic DNA. Translation: AAU03950.1.
RefSeqiYP_067432.1. NC_006142.1.

Genome annotation databases

EnsemblBacteriaiAAU03950; AAU03950; RT0478.
GeneIDi2959286.
KEGGirty:RT0478.
PATRICi17910198. VBIRicTyp34752_0507.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE017197 Genomic DNA. Translation: AAU03950.1 .
RefSeqi YP_067432.1. NC_006142.1.

3D structure databases

ProteinModelPortali Q68WP2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 257363.RT0478.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAU03950 ; AAU03950 ; RT0478 .
GeneIDi 2959286.
KEGGi rty:RT0478.
PATRICi 17910198. VBIRicTyp34752_0507.

Phylogenomic databases

eggNOGi COG0574.
HOGENOMi HOG000039664.
KOi K01006.
OMAi AVIYRKI.
OrthoDBi EOG6N0HGQ.

Enzyme and pathway databases

BioCyci RTYP257363:GJEQ-501-MONOMER.

Family and domain databases

Gene3Di 3.20.20.60. 1 hit.
3.30.1490.20. 2 hits.
3.30.470.20. 1 hit.
3.50.30.10. 1 hit.
InterProi IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR008279. PEP-util_enz_mobile_dom.
IPR018274. PEP_util_AS.
IPR000121. PEP_util_C.
IPR023151. PEP_util_CS.
IPR002192. PPDK_PEP-bd.
IPR010121. Pyruvate_phosphate_dikinase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view ]
PANTHERi PTHR22931:SF9. PTHR22931:SF9. 1 hit.
Pfami PF00391. PEP-utilizers. 1 hit.
PF02896. PEP-utilizers_C. 1 hit.
PF01326. PPDK_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000853. PPDK. 1 hit.
SUPFAMi SSF51621. SSF51621. 1 hit.
SSF52009. SSF52009. 1 hit.
TIGRFAMsi TIGR01828. pyru_phos_dikin. 1 hit.
PROSITEi PS00742. PEP_ENZYMES_2. 1 hit.
PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC VR-144 / Wilmington.

Entry informationi

Entry nameiPPDK_RICTY
AccessioniPrimary (citable) accession number: Q68WP2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: October 11, 2004
Last modified: May 14, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The reaction takes place in three steps, each mediated by a carrier histidine residue located on the surface of the central domain. The two first partial reactions are catalyzed at an active site located on the N-terminal domain, and the third partial reaction is catalyzed at an active site located on the C-terminal domain. For catalytic turnover, the central domain swivels from the concave surface of the N-terminal domain to that of the C-terminal domain.

Keywords - Technical termi

Complete proteome

Documents

  1. Rickettsia typhi
    Rickettsia typhi (strain Wilmington): entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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