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Conserved domains on  [gi|835736962|gb|AKM70347|]
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phosphoenolpyruvate carboxykinase, partial [Heuchera rubescens var. truncata]

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 ...
 1-76 3.75e-57

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 PLN02597:

Pssm-ID: 473983  Cd Length: 555  Bit Score: 183.07  E-value: 3.75e-57
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 835736962   1 VFVNDQFLNWDPEHRIKVRIVSARAYHSLFMHNMCIRPTPZELENFGTPDFTIYNAGQFPCNRYTHYMTSSTSIDL 76
Cdd:PLN02597 123 VFVNDQFLNWDPENRIKVRIVSARAYHSLFMHNMCIRPTPEELEDFGTPDFTIYNAGQFPCNRYTHYMTSSTSIDL 198
 
Name Accession Description Interval E-value
PLN02597 PLN02597
phosphoenolpyruvate carboxykinase [ATP]
 1-76 3.75e-57

phosphoenolpyruvate carboxykinase [ATP]


Pssm-ID: 178207  Cd Length: 555  Bit Score: 183.07  E-value: 3.75e-57
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 835736962   1 VFVNDQFLNWDPEHRIKVRIVSARAYHSLFMHNMCIRPTPZELENFGTPDFTIYNAGQFPCNRYTHYMTSSTSIDL 76
Cdd:PLN02597 123 VFVNDQFLNWDPENRIKVRIVSARAYHSLFMHNMCIRPTPEELEDFGTPDFTIYNAGQFPCNRYTHYMTSSTSIDL 198
PEPCK_ATP cd00484
Phosphoenolpyruvate carboxykinase (PEPCK), a critical gluconeogenic enzyme, catalyzes the ...
 1-76 6.97e-43

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) 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 ATP-dependent groups.


Pssm-ID: 238270  Cd Length: 508  Bit Score: 144.67  E-value: 6.97e-43
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 835736962   1 VFVNDQFLNWDPEHRIKVRIVSARAYHSLFMHNMCIRPTPZELENFGtPDFTIYNAGQFPCNRYTHYMTSSTSIDL 76
Cdd:cd00484   87 LFVFDGFAGADPEYRLKVRVITERAWHALFMRNMFIRPTEEELENFG-PDFTIYNAPKFKANPETDGMNSETFVII 161
PEPCK_ATP pfam01293
Phosphoenolpyruvate carboxykinase;
1-76 3.64e-35

Phosphoenolpyruvate carboxykinase;


Pssm-ID: 426184  Cd Length: 465  Bit Score: 123.30  E-value: 3.64e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 835736962    1 VFVNDQFLNWDPEHRIKVRIVSARAYHSLFMHNMCIRPTPZELENFgTPDFTIYNAGQFPCNRYTHYMTSSTSIDL 76
Cdd:pfam01293  87 LYVVDGFAGADPKYRLKVRVITERAWHALFARNMFIRPTEEELANF-EPDFTIINAPGFKADPERDGTNSETFIAL 161
PckA COG1866
Phosphoenolpyruvate carboxykinase, ATP-dependent [Energy production and conversion]; ...
 1-76 1.07e-29

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


Pssm-ID: 441471  Cd Length: 529  Bit Score: 109.01  E-value: 1.07e-29
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 835736962   1 VFVNDQFLNWDPEHRIKVRIVSARAYHSLFMHNMCIRPTPZELENFgTPDFTIYNAGQFPCNRYTHYMTSSTSIDL 76
Cdd:COG1866  104 LFVQDLYAGADPEYRLPVRVITEYAWHALFARNMFIRPTEEELANF-EPDFTIINAPGFKADPERDGTNSETFIIL 178
 
Name Accession Description Interval E-value
PLN02597 PLN02597
phosphoenolpyruvate carboxykinase [ATP]
 1-76 3.75e-57

phosphoenolpyruvate carboxykinase [ATP]


Pssm-ID: 178207  Cd Length: 555  Bit Score: 183.07  E-value: 3.75e-57
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 835736962   1 VFVNDQFLNWDPEHRIKVRIVSARAYHSLFMHNMCIRPTPZELENFGTPDFTIYNAGQFPCNRYTHYMTSSTSIDL 76
Cdd:PLN02597 123 VFVNDQFLNWDPENRIKVRIVSARAYHSLFMHNMCIRPTPEELEDFGTPDFTIYNAGQFPCNRYTHYMTSSTSIDL 198
PEPCK_ATP cd00484
Phosphoenolpyruvate carboxykinase (PEPCK), a critical gluconeogenic enzyme, catalyzes the ...
 1-76 6.97e-43

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) 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 ATP-dependent groups.


Pssm-ID: 238270  Cd Length: 508  Bit Score: 144.67  E-value: 6.97e-43
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 835736962   1 VFVNDQFLNWDPEHRIKVRIVSARAYHSLFMHNMCIRPTPZELENFGtPDFTIYNAGQFPCNRYTHYMTSSTSIDL 76
Cdd:cd00484   87 LFVFDGFAGADPEYRLKVRVITERAWHALFMRNMFIRPTEEELENFG-PDFTIYNAPKFKANPETDGMNSETFVII 161
PTZ00311 PTZ00311
phosphoenolpyruvate carboxykinase; Provisional
 1-76 3.84e-37

phosphoenolpyruvate carboxykinase; Provisional


Pssm-ID: 185549  Cd Length: 561  Bit Score: 129.78  E-value: 3.84e-37
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 835736962   1 VFVNDQFLNWDPEHRIKVRIVSARAYHSLFMHNMCIRPTPZELENFG---TPDFTIYNAGQFPCNRYTHYMTSSTSIDL 76
Cdd:PTZ00311 130 LFVVDGYAGWDPKYRLKVRVITTRAYHALFMRNMLIRPTNEELKKFGedfVPDFTIYNAGEFKANRLIEGVTSETSVAL 208
PEPCK_ATP pfam01293
Phosphoenolpyruvate carboxykinase;
1-76 3.64e-35

Phosphoenolpyruvate carboxykinase;


Pssm-ID: 426184  Cd Length: 465  Bit Score: 123.30  E-value: 3.64e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 835736962    1 VFVNDQFLNWDPEHRIKVRIVSARAYHSLFMHNMCIRPTPZELENFgTPDFTIYNAGQFPCNRYTHYMTSSTSIDL 76
Cdd:pfam01293  87 LYVVDGFAGADPKYRLKVRVITERAWHALFARNMFIRPTEEELANF-EPDFTIINAPGFKADPERDGTNSETFIAL 161
PckA COG1866
Phosphoenolpyruvate carboxykinase, ATP-dependent [Energy production and conversion]; ...
 1-76 1.07e-29

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


Pssm-ID: 441471  Cd Length: 529  Bit Score: 109.01  E-value: 1.07e-29
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 835736962   1 VFVNDQFLNWDPEHRIKVRIVSARAYHSLFMHNMCIRPTPZELENFgTPDFTIYNAGQFPCNRYTHYMTSSTSIDL 76
Cdd:COG1866  104 LFVQDLYAGADPEYRLPVRVITEYAWHALFARNMFIRPTEEELANF-EPDFTIINAPGFKADPERDGTNSETFIIL 178
PRK09344 PRK09344
phosphoenolpyruvate carboxykinase;
1-76 1.06e-25

phosphoenolpyruvate carboxykinase;


Pssm-ID: 236471  Cd Length: 526  Bit Score: 97.98  E-value: 1.06e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 835736962   1 VFVNDQFLNWDPEHRIKVRIVSARAYHSLFMHNMCIRPTPZELENFgTPDFTIYNAGQFPCNRYTHYMTSSTSIDL 76
Cdd:PRK09344 103 LFVVDGFAGADPEYRLPVRVITELAWHALFVRNLFIRPSEEELASF-EPDFTIINAPKFKADPERDGTNSETFIAI 177
PEPCK cd01919
Phosphoenolpyruvate carboxykinase (PEPCK), a critical gluconeogenic enzyme, catalyzes the ...
 1-60 3.22e-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).


Pssm-ID: 238900  Cd Length: 515  Bit Score: 71.12  E-value: 3.22e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 835736962   1 VFVNDQFLNWDPEHRIKVRIVSARAYHSLFMHNMCIRPTPZELENFGTPDFTIYNAGQFP 60
Cdd:cd01919   93 LFVVDFFMGPGSPLRLIVRELTDSPYVAAFMRIMTIMPTDEELAAFGDPDVKCLNSVGCP 152
 
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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