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Conserved domains on  [gi|38156134|gb|AAR12806|]
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cytosolic phosphoenolpyruvate carboxykinase, partial [Vidua orientalis aucupum]

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 ...
 1-30 1.40e-16

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 cd00819:

Pssm-ID: 473983  Cd Length: 579  Bit Score: 69.58  E-value: 1.40e-16
                        10        20        30
                ....*....|....*....|....*....|
gi 38156134   1 TAAAEHKGKIIMHDPFAMRPFFGYNFGKYL 30
Cdd:cd00819 429 TAAAEGKVGVVRRDPFAMLPFCGYNMGDYF 458
 
Name Accession Description Interval E-value
PEPCK_GTP cd00819
Phosphoenolpyruvate carboxykinase (PEPCK), a critical gluconeogenic enzyme, catalyzes the ...
 1-30 1.40e-16

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: 69.58  E-value: 1.40e-16
                        10        20        30
                ....*....|....*....|....*....|
gi 38156134   1 TAAAEHKGKIIMHDPFAMRPFFGYNFGKYL 30
Cdd:cd00819 429 TAAAEGKVGVVRRDPFAMLPFCGYNMGDYF 458
PEPCK_GTP pfam00821
Phosphoenolpyruvate carboxykinase C-terminal P-loop domain; catalyzes the formation of ...
 1-30 2.24e-15

Phosphoenolpyruvate carboxykinase C-terminal P-loop domain; catalyzes the formation of phosphoenolpyruvate by decarboxylation of oxaloacetate.


Pssm-ID: 459949  Cd Length: 356  Bit Score: 65.96  E-value: 2.24e-15
                          10        20        30
                  ....*....|....*....|....*....|
gi 38156134     1 TAAAEHKGKIIMHDPFAMRPFFGYNFGKYL 30
Cdd:pfam00821 204 TAAAEGKVGVVRRDPMAMLPFCGYNMGDYL 233
PepCK COG1274
Phosphoenolpyruvate carboxykinase, GTP-dependent [Energy production and conversion]; ...
 1-30 3.19e-08

Phosphoenolpyruvate carboxykinase, GTP-dependent [Energy production and conversion]; Phosphoenolpyruvate carboxykinase, GTP-dependent is part of the Pathway/BioSystem: Gluconeogenesis


Pssm-ID: 440885  Cd Length: 605  Bit Score: 45.91  E-value: 3.19e-08
                        10        20        30
                ....*....|....*....|....*....|
gi 38156134   1 TAAAEHKGKIIMHDPFAMRPFFGYNFGKYL 30
Cdd:COG1274 448 TAAAEGAVGVVRRDPFAMLPFCGYNMGDYF 477
PRK04210 PRK04210
phosphoenolpyruvate carboxykinase (GTP);
1-30 6.22e-08

phosphoenolpyruvate carboxykinase (GTP);


Pssm-ID: 235256  Cd Length: 601  Bit Score: 44.82  E-value: 6.22e-08
                         10        20        30
                 ....*....|....*....|....*....|
gi 38156134    1 TAAAEHKGKIIMHDPFAMRPFFGYNFGKYL 30
Cdd:PRK04210 443 TAAAEGKVGVVRRDPMAMLPFCGYNMGDYF 472
 
Name Accession Description Interval E-value
PEPCK_GTP cd00819
Phosphoenolpyruvate carboxykinase (PEPCK), a critical gluconeogenic enzyme, catalyzes the ...
 1-30 1.40e-16

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: 69.58  E-value: 1.40e-16
                        10        20        30
                ....*....|....*....|....*....|
gi 38156134   1 TAAAEHKGKIIMHDPFAMRPFFGYNFGKYL 30
Cdd:cd00819 429 TAAAEGKVGVVRRDPFAMLPFCGYNMGDYF 458
PEPCK_GTP pfam00821
Phosphoenolpyruvate carboxykinase C-terminal P-loop domain; catalyzes the formation of ...
 1-30 2.24e-15

Phosphoenolpyruvate carboxykinase C-terminal P-loop domain; catalyzes the formation of phosphoenolpyruvate by decarboxylation of oxaloacetate.


Pssm-ID: 459949  Cd Length: 356  Bit Score: 65.96  E-value: 2.24e-15
                          10        20        30
                  ....*....|....*....|....*....|
gi 38156134     1 TAAAEHKGKIIMHDPFAMRPFFGYNFGKYL 30
Cdd:pfam00821 204 TAAAEGKVGVVRRDPMAMLPFCGYNMGDYL 233
PEPCK cd01919
Phosphoenolpyruvate carboxykinase (PEPCK), a critical gluconeogenic enzyme, catalyzes the ...
 3-30 3.69e-10

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: 51.47  E-value: 3.69e-10
                        10        20
                ....*....|....*....|....*...
gi 38156134   3 AAEHKGKIIMHDPFAMRPFFGYNFGKYL 30
Cdd:cd01919 371 EAGHKGKIPMFSPCFGRPFLGYHFTKYL 398
PepCK COG1274
Phosphoenolpyruvate carboxykinase, GTP-dependent [Energy production and conversion]; ...
 1-30 3.19e-08

Phosphoenolpyruvate carboxykinase, GTP-dependent [Energy production and conversion]; Phosphoenolpyruvate carboxykinase, GTP-dependent is part of the Pathway/BioSystem: Gluconeogenesis


Pssm-ID: 440885  Cd Length: 605  Bit Score: 45.91  E-value: 3.19e-08
                        10        20        30
                ....*....|....*....|....*....|
gi 38156134   1 TAAAEHKGKIIMHDPFAMRPFFGYNFGKYL 30
Cdd:COG1274 448 TAAAEGAVGVVRRDPFAMLPFCGYNMGDYF 477
PRK04210 PRK04210
phosphoenolpyruvate carboxykinase (GTP);
1-30 6.22e-08

phosphoenolpyruvate carboxykinase (GTP);


Pssm-ID: 235256  Cd Length: 601  Bit Score: 44.82  E-value: 6.22e-08
                         10        20        30
                 ....*....|....*....|....*....|
gi 38156134    1 TAAAEHKGKIIMHDPFAMRPFFGYNFGKYL 30
Cdd:PRK04210 443 TAAAEGKVGVVRRDPMAMLPFCGYNMGDYF 472
 
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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