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Conserved domains on  [gi|57648838|gb|AAW55972|]
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PEPCK, partial [Corynorhinus townsendii]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PEPCK_HprK super family cl22860
Phosphoenolpyruvate carboxykinase (PEPCK), a critical gluconeogenic enzyme, catalyzes the ...
1-19 7.50e-05

Phosphoenolpyruvate carboxykinase (PEPCK), a critical gluconeogenic enzyme, catalyzes the first committed step in the diversion of tricarboxylic acid cycle intermediates toward gluconeogenesis. It catalyzes the reversible decarboxylation and phosphorylation of oxaloacetate to yield phosphoenolpyruvate and carbon dioxide, using a nucleotide molecule (ATP or GTP) for the phosphoryl transfer, and has a strict requirement for divalent metal ions for activity. PEPCK's separate into two phylogenetic groups based on their nucleotide substrate specificity (the ATP-, and GTP-dependent groups).HprK/P, the bifunctional histidine-containing protein kinase/phosphatase, controls the phosphorylation state of the phosphocarrier protein HPr and regulates the utilization of carbon sources by gram-positive bacteria. It catalyzes both the ATP-dependent phosphorylation of HPr and its dephosphorylation by phosphorolysis. PEPCK and the C-terminal catalytic domain of HprK/P are structurally similar with conserved active site residues suggesting that these two phosphotransferases have related functions.


The actual alignment was detected with superfamily member cd01919:

Pssm-ID: 473983  Cd Length: 515  Bit Score: 35.68  E-value: 7.50e-05
                        10
                ....*....|....*....
gi 57648838   1 MSEEDFEKAFSARFPGCMK 19
Cdd:cd01919  71 LSEEDFEKAFNARFPGLMK 89
 
Name Accession Description Interval E-value
PEPCK cd01919
Phosphoenolpyruvate carboxykinase (PEPCK), a critical gluconeogenic enzyme, catalyzes the ...
1-19 7.50e-05

Phosphoenolpyruvate carboxykinase (PEPCK), a critical gluconeogenic enzyme, catalyzes the first committed step in the diversion of tricarboxylic acid cycle intermediates toward gluconeogenesis. It catalyzes the reversible decarboxylation and phosphorylation of oxaloacetate to yield phosphoenolpyruvate and carbon dioxide, using a nucleotide molecule (ATP or GTP) for the phosphoryl transfer, and has a strict requirement for divalent metal ions for activity. PEPCK's separate into two phylogenetic groups based on their nucleotide substrate specificity (the ATP-, and GTP-dependent groups).


Pssm-ID: 238900  Cd Length: 515  Bit Score: 35.68  E-value: 7.50e-05
                        10
                ....*....|....*....
gi 57648838   1 MSEEDFEKAFSARFPGCMK 19
Cdd:cd01919  71 LSEEDFEKAFNARFPGLMK 89
 
Name Accession Description Interval E-value
PEPCK cd01919
Phosphoenolpyruvate carboxykinase (PEPCK), a critical gluconeogenic enzyme, catalyzes the ...
1-19 7.50e-05

Phosphoenolpyruvate carboxykinase (PEPCK), a critical gluconeogenic enzyme, catalyzes the first committed step in the diversion of tricarboxylic acid cycle intermediates toward gluconeogenesis. It catalyzes the reversible decarboxylation and phosphorylation of oxaloacetate to yield phosphoenolpyruvate and carbon dioxide, using a nucleotide molecule (ATP or GTP) for the phosphoryl transfer, and has a strict requirement for divalent metal ions for activity. PEPCK's separate into two phylogenetic groups based on their nucleotide substrate specificity (the ATP-, and GTP-dependent groups).


Pssm-ID: 238900  Cd Length: 515  Bit Score: 35.68  E-value: 7.50e-05
                        10
                ....*....|....*....
gi 57648838   1 MSEEDFEKAFSARFPGCMK 19
Cdd:cd01919  71 LSEEDFEKAFNARFPGLMK 89
PEPCK_GTP cd00819
Phosphoenolpyruvate carboxykinase (PEPCK), a critical gluconeogenic enzyme, catalyzes the ...
1-19 3.62e-03

Phosphoenolpyruvate carboxykinase (PEPCK), a critical gluconeogenic enzyme, catalyzes the first committed step in the diversion of tricarboxylic acid cycle intermediates toward gluconeogenesis. It catalyzes the reversible decarboxylation and phosphorylation of oxaloacetate to yield phosphoenolpyruvate and carbon dioxide, using a nucleotide molecule (GTP) for the phosphoryl transfer, and has a strict requirement for divalent metal ions for activity. PEPCK's separate into two phylogenetic groups based on their nucleotide substrate specificity, this model describes the GTP-dependent group.


Pssm-ID: 238417  Cd Length: 579  Bit Score: 30.67  E-value: 3.62e-03
                        10
                ....*....|....*....
gi 57648838   1 MSEEDFEKAFSARFPGCMK 19
Cdd:cd00819  83 MDPEEMKAELKELFKGCMR 101
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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