Q59754 · PPDK_RHIME

Function

function

Catalyzes the reversible phosphorylation of pyruvate and phosphate.

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.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Activity regulation

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

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site96ATP (UniProtKB | ChEBI)
Active site468Tele-phosphohistidine intermediate
Binding site574substrate
Binding site630substrate
Binding site758Mg2+ (UniProtKB | ChEBI)
Binding site758substrate
Binding site779substrate
Binding site780substrate
Binding site781substrate
Binding site782Mg2+ (UniProtKB | ChEBI)
Binding site782substrate
Active site844Proton donor

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular Functionkinase activity
Molecular Functionmetal ion binding
Molecular Functionpyruvate, phosphate dikinase activity
Biological Processphosphorylation
Biological Processpyruvate metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Pyruvate, phosphate dikinase
  • EC number
  • Alternative names
    • Pyruvate, orthophosphate dikinase

Gene names

    • Name
      ppdK
    • Synonyms
      podA
    • ORF names
      SMc00025
    • Ordered locus names
      R00932

Organism names

Accessions

  • Primary accession
    Q59754
  • Secondary accessions
    • Q59755
    • Q59756

Proteomes

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001470471-898Pyruvate, phosphate dikinase
Modified residue466Phosphothreonine; by PDRP1

Post-translational modification

Phosphorylation of Thr-466 in the dark inactivates the enzyme. Dephosphorylation upon light stimulation reactivates the enzyme (By similarity).

Keywords

Interaction

Subunit

Homodimer.

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-355N-terminal
Region356-412Linker 1
Region413-511Central
Region512-546Linker 2
Region547-898C-terminal

Domain

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.

Sequence similarities

Belongs to the PEP-utilizing enzyme family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    898
  • Mass (Da)
    97,561
  • Last updated
    2000-05-30 v2
  • Checksum
    D055560636388CD5
MAKWVYTFGAGQAEGSAEDRDRLGGKGANLAEMCNLGLPVPPGLTIVTAACNSYLEKGRSMPEGLREQVREGITRMEKITGRVFGDTNRPLLLSVRSGARASMPGMMDTVLNLGLNDQSVHALGHDAGDARFAWDSYRRFIQMYGDVVMGVDHEVFEEVLEDEKARLGHEQDTELSAVEWQHVISRYKEAIEEVLGLPFPQDPEVQLWGAIGAVFSSWMNPRAITYRHLHGIPAGWGTAVNVQAMVFGNLGNSSATGVAFTRNPSTGEKELYGEFLVNAQGEDVVAGIRTPQNITEAARIASGSDKPSLEKLMPEAFAEFEKICNALERHYRDMQDIEFTIERGKLWMLQTRSGKRTAKSALKIAVDMAEEGLISKEEAVARIDPASLDQLLHPTIDPHARRDIIGSGLPASPGAATGEIVFSSDEAVQAVKEGRKVILVRVETSPEDIHGMHAAEGILTTRGGMTSHAAVVARGMGTPCVSGAGSIRVDQRNELLIAASVTLRKGDVITIDGSSGQVLKGEIPMLQPELSGDFGKIMQWADASRRMTVRTNAETPADARAARSFGAEGIGLCRTEHMFFEDDRINVMREMILAEDEAGRRTALAKLLPMQRSDFVELFSIMHGLPVTIRLLDPPLHEFLPKTDEEIAEVARVLTIDPAELRQRVDALHEFNPMLGHRGCRLAISYPEIAEMQARAIFEAAVQAAHDTGAAVVPEIMVPLVGLRAELDYVKARIEAVAKEVIGEAGVNIDYLIGTMIELPRAALRADTIAESADFFSFGTNDLTQTTFGISRDDAALFLATYQQKGIIEQDPFVSLDFEGVGELIQIAAERGRRTKNGLKLGICGEHGGDPASIRFCEEAGLDYVSCSPFRVPIARLAAAQATINGREVAEVQALAAS

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict88in Ref. 3; AAB58818
Sequence conflict128in Ref. 3; AAB58818
Sequence conflict711-712in Ref. 3
Sequence conflict722-723in Ref. 3
Sequence conflict736-738in Ref. 3; AAB58820

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL591688
EMBL· GenBank· DDBJ
CAC45504.1
EMBL· GenBank· DDBJ
Genomic DNA
AH005244
EMBL· GenBank· DDBJ
AAB58818.1
EMBL· GenBank· DDBJ
Genomic DNA
AH005244
EMBL· GenBank· DDBJ
AAB58819.1
EMBL· GenBank· DDBJ
Genomic DNA
AH005244
EMBL· GenBank· DDBJ
AAB58820.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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