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Conserved domains on  [gi|2462574278|ref|XP_054198513|]
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pyruvate dehydrogenase (acetyl-transferring) kinase isozyme 1, mitochondrial isoform X3 [Homo sapiens]

Protein Classification

BCDHK_Adom3 domain-containing protein( domain architecture ID 10564471)

BCDHK_Adom3 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BCDHK_Adom3 pfam10436
Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of ...
 56-240 6.51e-63

Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of leucine, isoleucine and valine are finely balanced, allowing the body to make the most of dietary input but removing excesses to prevent toxic build-up of their corresponding keto-acids. This is the butyryl-CoA dehydrogenase, subunit A domain 3, a largely alpha-helical bundle of the enzyme BCDHK. This enzyme is the regulator of the dehydrogenase complex that breaks branched-chain amino-acids down, by phosphorylating and thereby inactivating it when synthesis is required. The domain is associated with family HATPase_c pfam02518 which is towards the C-terminal.


:

Pssm-ID: 463093  Cd Length: 158  Bit Score: 195.80  E-value: 6.51e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574278  56 PLSMKQFLDFGSVNACEKT--SFMFLRQELPVRLANIMKEISLLPDNLLRTPSVQLVQSWYIQSLQELLDFKDKSAEDAK 133
Cdd:pfam10436   1 PLSLRQLLDFGRSLSEEKLlkSANFLREELPVRLAHRIRELQNLPYILVSNPSISKVYEWYLQSFEELLSFPPPILEDNE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574278 134 AiyerprrtwlqvsslccmackmiFTDTVIRIRNRHNDVIPTMAQGVIEYKESfgvdpVTSQNVQYFLDRFYMSRISIRM 213
Cdd:pfam10436  81 K-----------------------FTELLEEILDRHNDVVPTLAQGVLELKKY-----LSPEEIQSFLDRFLRSRIGIRL 132

                         170       180
                  ....*....|....*....|....*..
gi 2462574278 214 LLNQHSLLFGGKgKGSPSHRKHIGSIN 240
Cdd:pfam10436 133 LAEQHIALTEQS-NNPSHPPDYVGIID 158
HATPase super family cl00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
 244-268 1.26e-03

Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ATPase (HATPase) domains of several ATP-binding proteins such as histidine kinase, DNA gyrase B, topoisomerases, heat shock protein 90 (HSP90), phytochrome-like ATPases and DNA mismatch repair proteins. Domains belonging to this superfamily are also referred to as GHKL (gyrase, heat-shock protein 90, histidine kinase, MutL) ATPase domains.


The actual alignment was detected with superfamily member cd16929:

Pssm-ID: 469604 [Multi-domain]  Cd Length: 169  Bit Score: 38.86  E-value: 1.26e-03
                          10        20
                  ....*....|....*....|....*
gi 2462574278 244 NVLEVIKDGYENARRLCDLYYINSP 268
Cdd:cd16929     1 SPKKVVEDASEEARVLCDDYYLSSP 25
 
Name Accession Description Interval E-value
BCDHK_Adom3 pfam10436
Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of ...
 56-240 6.51e-63

Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of leucine, isoleucine and valine are finely balanced, allowing the body to make the most of dietary input but removing excesses to prevent toxic build-up of their corresponding keto-acids. This is the butyryl-CoA dehydrogenase, subunit A domain 3, a largely alpha-helical bundle of the enzyme BCDHK. This enzyme is the regulator of the dehydrogenase complex that breaks branched-chain amino-acids down, by phosphorylating and thereby inactivating it when synthesis is required. The domain is associated with family HATPase_c pfam02518 which is towards the C-terminal.


Pssm-ID: 463093  Cd Length: 158  Bit Score: 195.80  E-value: 6.51e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574278  56 PLSMKQFLDFGSVNACEKT--SFMFLRQELPVRLANIMKEISLLPDNLLRTPSVQLVQSWYIQSLQELLDFKDKSAEDAK 133
Cdd:pfam10436   1 PLSLRQLLDFGRSLSEEKLlkSANFLREELPVRLAHRIRELQNLPYILVSNPSISKVYEWYLQSFEELLSFPPPILEDNE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574278 134 AiyerprrtwlqvsslccmackmiFTDTVIRIRNRHNDVIPTMAQGVIEYKESfgvdpVTSQNVQYFLDRFYMSRISIRM 213
Cdd:pfam10436  81 K-----------------------FTELLEEILDRHNDVVPTLAQGVLELKKY-----LSPEEIQSFLDRFLRSRIGIRL 132

                         170       180
                  ....*....|....*....|....*..
gi 2462574278 214 LLNQHSLLFGGKgKGSPSHRKHIGSIN 240
Cdd:pfam10436 133 LAEQHIALTEQS-NNPSHPPDYVGIID 158
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
 244-268 1.26e-03

Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain alpha-ketoacid dehydrogenase kinase and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of all four PDK isoforms (pyruvate dehydrogenase kinases 1-4) that have been described in mammals, and other PDKs including Saccharomyces Pkp1p and Pkp2p. PDKs and phosphatases tightly regulate the mitochondrial pyruvate dehydrogenase complex (PDC) by reversible phosphorylation. PDC catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA, connecting glycolysis and the TCA acid cycle. Also included in this family is mammalian branched-chain alpha-ketoacid dehydrogenase kinase (BDK), a mitochondrial protein kinase that phosphorylates a subunit of the branched-chain a-ketoacid dehydrogenase (BCKD) complex, which catalyzes the oxidative decarboxylation of branched-chain alpha-ketoacids derived from leucine, isoleucine, and valine, a rate-limiting step in the oxidative degradation of these branched-chain amino acids.


Pssm-ID: 340406 [Multi-domain]  Cd Length: 169  Bit Score: 38.86  E-value: 1.26e-03
                          10        20
                  ....*....|....*....|....*
gi 2462574278 244 NVLEVIKDGYENARRLCDLYYINSP 268
Cdd:cd16929     1 SPKKVVEDASEEARVLCDDYYLSSP 25
 
Name Accession Description Interval E-value
BCDHK_Adom3 pfam10436
Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of ...
 56-240 6.51e-63

Mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase; Catabolism and synthesis of leucine, isoleucine and valine are finely balanced, allowing the body to make the most of dietary input but removing excesses to prevent toxic build-up of their corresponding keto-acids. This is the butyryl-CoA dehydrogenase, subunit A domain 3, a largely alpha-helical bundle of the enzyme BCDHK. This enzyme is the regulator of the dehydrogenase complex that breaks branched-chain amino-acids down, by phosphorylating and thereby inactivating it when synthesis is required. The domain is associated with family HATPase_c pfam02518 which is towards the C-terminal.


Pssm-ID: 463093  Cd Length: 158  Bit Score: 195.80  E-value: 6.51e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574278  56 PLSMKQFLDFGSVNACEKT--SFMFLRQELPVRLANIMKEISLLPDNLLRTPSVQLVQSWYIQSLQELLDFKDKSAEDAK 133
Cdd:pfam10436   1 PLSLRQLLDFGRSLSEEKLlkSANFLREELPVRLAHRIRELQNLPYILVSNPSISKVYEWYLQSFEELLSFPPPILEDNE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462574278 134 AiyerprrtwlqvsslccmackmiFTDTVIRIRNRHNDVIPTMAQGVIEYKESfgvdpVTSQNVQYFLDRFYMSRISIRM 213
Cdd:pfam10436  81 K-----------------------FTELLEEILDRHNDVVPTLAQGVLELKKY-----LSPEEIQSFLDRFLRSRIGIRL 132

                         170       180
                  ....*....|....*....|....*..
gi 2462574278 214 LLNQHSLLFGGKgKGSPSHRKHIGSIN 240
Cdd:pfam10436 133 LAEQHIALTEQS-NNPSHPPDYVGIID 158
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
 244-268 1.26e-03

Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain alpha-ketoacid dehydrogenase kinase and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of all four PDK isoforms (pyruvate dehydrogenase kinases 1-4) that have been described in mammals, and other PDKs including Saccharomyces Pkp1p and Pkp2p. PDKs and phosphatases tightly regulate the mitochondrial pyruvate dehydrogenase complex (PDC) by reversible phosphorylation. PDC catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA, connecting glycolysis and the TCA acid cycle. Also included in this family is mammalian branched-chain alpha-ketoacid dehydrogenase kinase (BDK), a mitochondrial protein kinase that phosphorylates a subunit of the branched-chain a-ketoacid dehydrogenase (BCKD) complex, which catalyzes the oxidative decarboxylation of branched-chain alpha-ketoacids derived from leucine, isoleucine, and valine, a rate-limiting step in the oxidative degradation of these branched-chain amino acids.


Pssm-ID: 340406 [Multi-domain]  Cd Length: 169  Bit Score: 38.86  E-value: 1.26e-03
                          10        20
                  ....*....|....*....|....*
gi 2462574278 244 NVLEVIKDGYENARRLCDLYYINSP 268
Cdd:cd16929     1 SPKKVVEDASEEARVLCDDYYLSSP 25
 
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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