2-oxoglutarate dehydrogenase component E1 family protein may catalyzes the decarboxylation of 2-oxoglutarate and the formation of TPP-hydroxysuccinate or the conversion of 2-oxoadipate (alpha-ketoadipate) to glutaryl-CoA and CO(2).
2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component, and related enzymes ...
1-472
0e+00
2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component, and related enzymes [Energy production and conversion]; 2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component, and related enzymes is part of the Pathway/BioSystem: TCA cycle
The actual alignment was detected with superfamily member COG0567:
Pssm-ID: 440333 [Multi-domain] Cd Length: 935 Bit Score: 670.25 E-value: 0e+00
2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component, and related enzymes ...
1-472
0e+00
2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component, and related enzymes [Energy production and conversion]; 2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component, and related enzymes is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440333 [Multi-domain] Cd Length: 935 Bit Score: 670.25 E-value: 0e+00
2-oxoglutarate dehydrogenase, E1 component; The 2-oxoglutarate dehydrogenase complex consists ...
1-471
4.68e-165
2-oxoglutarate dehydrogenase, E1 component; The 2-oxoglutarate dehydrogenase complex consists of this thiamine pyrophosphate-binding subunit (E1), dihydrolipoamide succinyltransferase (E2), and lipoamide dehydrogenase (E3). The E1 ortholog from Corynebacterium glutamicum is unusual in having an N-terminal extension that resembles the dihydrolipoamide succinyltransferase (E2) component of 2-oxoglutarate dehydrogenase. [Energy metabolism, TCA cycle]
Pssm-ID: 161785 [Multi-domain] Cd Length: 929 Bit Score: 489.77 E-value: 4.68e-165
2-oxoglutarate dehydrogenase C-terminal; OxoGdeHyase_C is a family found immediately ...
329-471
6.16e-73
2-oxoglutarate dehydrogenase C-terminal; OxoGdeHyase_C is a family found immediately C-terminal to Transket_pyr, pfam02779. It is found at the C-terminus of 2-oxoglutarate dehydrogenase.
Pssm-ID: 465289 [Multi-domain] Cd Length: 147 Bit Score: 226.55 E-value: 6.16e-73
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ...
188-324
6.16e-27
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.
Pssm-ID: 214865 [Multi-domain] Cd Length: 136 Bit Score: 105.26 E-value: 6.16e-27
2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component, and related enzymes ...
1-472
0e+00
2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component, and related enzymes [Energy production and conversion]; 2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component, and related enzymes is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440333 [Multi-domain] Cd Length: 935 Bit Score: 670.25 E-value: 0e+00
2-oxoglutarate dehydrogenase, E1 component; The 2-oxoglutarate dehydrogenase complex consists ...
1-471
4.68e-165
2-oxoglutarate dehydrogenase, E1 component; The 2-oxoglutarate dehydrogenase complex consists of this thiamine pyrophosphate-binding subunit (E1), dihydrolipoamide succinyltransferase (E2), and lipoamide dehydrogenase (E3). The E1 ortholog from Corynebacterium glutamicum is unusual in having an N-terminal extension that resembles the dihydrolipoamide succinyltransferase (E2) component of 2-oxoglutarate dehydrogenase. [Energy metabolism, TCA cycle]
Pssm-ID: 161785 [Multi-domain] Cd Length: 929 Bit Score: 489.77 E-value: 4.68e-165
2-oxoglutarate dehydrogenase C-terminal; OxoGdeHyase_C is a family found immediately ...
329-471
6.16e-73
2-oxoglutarate dehydrogenase C-terminal; OxoGdeHyase_C is a family found immediately C-terminal to Transket_pyr, pfam02779. It is found at the C-terminus of 2-oxoglutarate dehydrogenase.
Pssm-ID: 465289 [Multi-domain] Cd Length: 147 Bit Score: 226.55 E-value: 6.16e-73
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ...
120-324
4.31e-56
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate dehydrogenases, and branched chain alpha-keto acid decarboxylases.
Pssm-ID: 460692 [Multi-domain] Cd Length: 174 Bit Score: 184.29 E-value: 4.31e-56
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ...
188-324
6.16e-27
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.
Pssm-ID: 214865 [Multi-domain] Cd Length: 136 Bit Score: 105.26 E-value: 6.16e-27
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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