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InterPro: IPR001017 Dehydrogenase, E1 component
Protein matches
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UniProtKB Matches: 3815 proteins |
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Accession
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IPR001017 DH_E1 |
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Type
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Domain |
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Signatures
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InterPro Relationships
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Found in
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IPR011603 2-oxoglutarate dehydrogenase, E1 component
IPR017596 Pyruvate dehydrogenase (acetyl-transferring) E1 component, alpha subunit subgroup x
IPR017597 Pyruvate dehydrogenase (acetyl-transferring) E1 component, alpha subunit, subgroup y
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GO Term annotation
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Process
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GO:0008152 metabolic process
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Function
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GO:0016624 oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
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InterPro annotation
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 Entry Details in BioMart
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Abstract
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This entry includes a number of dehydrogenases all of which use thiamine
pyrophosphate as a cofactor and are members of a multienzyme complex.
Pyruvate dehydrogenase (EC:1.2.4.1), a component of the multienzyme
pyruvate dehydrogenase complex; 2-oxoglutarate dehydrogenase (EC:1.2.4.2),
a component of the multienzyme 2-oxoglutarate dehydrogenase which contains
multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1),
dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3);
and 2-oxoisovalerate dehydrogenase (EC:1.2.4.4), a component of the multienzyme
branched-chain alpha-keto dehydrogenase complex all belong to this family.
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Structural links
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Database links
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Pfam Clan: CL0254.5
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Example proteins
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A2ATU0 Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1, mitochondrial
O61199 2-oxoglutarate dehydrogenase E1 component, mitochondrial
P08559 Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
P16387 Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial
Q9VA02 Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1 homolog, mitochondrial
More proteins
Example Proteins Key
| InterPro entry accession number/name and structure databases |
Colour code |
| IPR017597 |
Pyruvate dehydrogenase (acetyl-transferring) E1 component, alpha subunit, subgroup y |
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| IPR005475 |
Transketolase-like, pyrimidine-binding domain |
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| IPR011603 |
2-oxoglutarate dehydrogenase, E1 component |
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| IPR001017 |
Dehydrogenase, E1 component |
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SWISS-MODEL |
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PDB Chain |
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ModBase |
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SCOP Domain |
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CATH Domain |
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Additional Reading
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Frank RA, Pratap JV, Pei XY, Perham RN, Luisi BF.
The molecular origins of specificity in the assembly of a multienzyme complex.
Structure 13 2005 1119-30
[PubMed: 16084384]
http://dx.doi.org/10.1016/j.str.2005.04.021
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Nakai T, Nakagawa N, Maoka N, Masui R, Kuramitsu S, Kamiya N.
Ligand-induced conformational changes and a reaction intermediate in branched-chain 2-oxo acid dehydrogenase (E1) from Thermus thermophilus HB8, as revealed by X-ray crystallography.
J. Mol. Biol. 337 2004 1011-33
[PubMed: 15033367]
http://dx.doi.org/10.1016/j.jmb.2004.02.011
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Seifert F, Ciszak E, Korotchkina L, Golbik R, Spinka M, Dominiak P, Sidhu S, Brauer J, Patel MS, Tittmann K.
Phosphorylation of serine 264 impedes active site accessibility in the E1 component of the human pyruvate dehydrogenase multienzyme complex.
Biochemistry 46 2007 6277-87
[PubMed: 17474719]
http://dx.doi.org/10.1021/bi700083z
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Wynn RM, Kato M, Machius M, Chuang JL, Li J, Tomchick DR, Chuang DT.
Molecular mechanism for regulation of the human mitochondrial branched-chain alpha-ketoacid dehydrogenase complex by phosphorylation.
Structure 12 2004 2185-96
[PubMed: 15576032]
http://dx.doi.org/10.1016/j.str.2004.09.013
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Machius M, Wynn RM, Chuang JL, Li J, Kluger R, Yu D, Tomchick DR, Brautigam CA, Chuang DT.
A versatile conformational switch regulates reactivity in human branched-chain alpha-ketoacid dehydrogenase.
Structure 14 2006 287-98
[PubMed: 16472748]
http://dx.doi.org/10.1016/j.str.2005.10.009
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InterPro 23.1
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