General Information of Protein (ID: PRT01140)
Name Alpha-ketoglutarate dehydrogenase (OGDH)
Synonyms   Click to Show/Hide Synonyms of This Protein
2-oxoglutarate dehydrogenase complex component E1; OGDC-E1; Alpha-ketoglutarate dehydrogenase; OGDH
Gene Name OGDH Gene ID
4967
UniProt ID
Q02218
Family Oxidoreductases (EC 1)
EC Number   EC: 1.2.4.2  (Click to Show/Hide the Complete EC Tree)
Oxidoreductase
Aldehyde/oxo donor oxidoreductase
Disulfide acceptor oxidoreductase
EC: 1.2.4.2
  Click to Show/Hide the Molecular/Functional Data (Sequence/Structure/Function) of This Protein
Sequence
MFHLRTCAAKLRPLTASQTVKTFSQNRPAAARTFQQIRCYSAPVAAEPFLSGTSSNYVEE
MYCAWLENPKSVHKSWDIFFRNTNAGAPPGTAYQSPLPLSRGSLAAVAHAQSLVEAQPNV
DKLVEDHLAVQSLIRAYQIRGHHVAQLDPLGILDADLDSSVPADIISSTDKLGFYGLDES
DLDKVFHLPTTTFIGGQESALPLREIIRRLEMAYCQHIGVEFMFINDLEQCQWIRQKFET
PGIMQFTNEEKRTLLARLVRSTRFEEFLQRKWSSEKRFGLEGCEVLIPALKTIIDKSSEN
GVDYVIMGMPHRGRLNVLANVIRKELEQIFCQFDSKLEAADEGSGDVKYHLGMYHRRINR
VTDRNITLSLVANPSHLEAADPVVMGKTKAEQFYCGDTEGKKVMSILLHGDAAFAGQGIV
YETFHLSDLPSYTTHGTVHVVVNNQIGFTTDPRMARSSPYPTDVARVVNAPIFHVNSDDP
EAVMYVCKVAAEWRSTFHKDVVVDLVCYRRNGHNEMDEPMFTQPLMYKQIRKQKPVLQKY
AELLVSQGVVNQPEYEEEISKYDKICEEAFARSKDEKILHIKHWLDSPWPGFFTLDGQPR
SMSCPSTGLTEDILTHIGNVASSVPVENFTIHGGLSRILKTRGEMVKNRTVDWALAEYMA
FGSLLKEGIHIRLSGQDVERGTFSHRHHVLHDQNVDKRTCIPMNHLWPNQAPYTVCNSSL
SEYGVLGFELGFAMASPNALVLWEAQFGDFHNTAQCIIDQFICPGQAKWVRQNGIVLLLP
HGMEGMGPEHSSARPERFLQMCNDDPDVLPDLKEANFDINQLYDCNWVVVNCSTPGNFFH
VLRRQILLPFRKPLIIFTPKSLLRHPEARSSFDEMLPGTHFQRVIPEDGPAAQNPENVKR
LLFCTGKVYYDLTRERKARDMVGQVAITRIEQLSPFPFDLLLKEVQKYPNAELAWCQEEH
KNQGYYDYVKPRLRTTISRAKPVWYAGRDPAAAPATGNKKTHLTELQRLLDTAFDLDVFK
NFS
Structure
3ERY
Function 2-oxoglutarate dehydrogenase (E1) component of the 2-oxoglutarate dehydrogenase complex (OGDHC), which mediates the decarboxylation of alpha-ketoglutarate. The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion. A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A.
Regulatory Network
Full List of Metabolite(s) Regulated by This Protein
      Organic acids and derivatives
            2-Hydroxyglutarate Click to Show/Hide the Full List of Regulating Pair(s):   1 Pair(s)
               Detailed Information Metabo  Info click to show the details of this metabolite
               Regulating Pair Experim Info click to show the details of experiment for validating this pair [1]
                      Introduced Variation Knockout of OGDH
                      Induced Change 2-Hydroxyglutarate concentration: increase
                      Summary Introduced Variation         Induced Change 
                      Disease Status Cervical Cancer [ICD-11: 2C77]
                      Details It is reported that knockout of OGDH leads to the increase of 2-hydroxyglutarate levels compared with control group.
            Citric acid Click to Show/Hide the Full List of Regulating Pair(s):   1 Pair(s)
               Detailed Information Metabo  Info click to show the details of this metabolite
               Regulating Pair Experim Info click to show the details of experiment for validating this pair [1]
                      Introduced Variation Knockout of OGDH
                      Induced Change Citric acid concentration: decrease
                      Summary Introduced Variation         Induced Change 
                      Disease Status Cervical Cancer [ICD-11: 2C77]
                      Details It is reported that knockout of OGDH leads to the decrease of citric acid levels compared with control group.
            Malic acid Click to Show/Hide the Full List of Regulating Pair(s):   1 Pair(s)
               Detailed Information Metabo  Info click to show the details of this metabolite
               Regulating Pair Experim Info click to show the details of experiment for validating this pair [1]
                      Introduced Variation Knockout of OGDH
                      Induced Change Malic acid concentration: decrease
                      Summary Introduced Variation         Induced Change 
                      Disease Status Cervical Cancer [ICD-11: 2C77]
                      Details It is reported that knockout of OGDH leads to the decrease of malic acid levels compared with control group.
            Oxoglutaric acid Click to Show/Hide the Full List of Regulating Pair(s):   1 Pair(s)
               Detailed Information Metabo  Info click to show the details of this metabolite
               Regulating Pair Experim Info click to show the details of experiment for validating this pair [1]
                      Introduced Variation Knockout of OGDH
                      Induced Change Oxoglutaric acid concentration: increase
                      Summary Introduced Variation         Induced Change 
                      Disease Status Cervical Cancer [ICD-11: 2C77]
                      Details It is reported that knockout of OGDH leads to the increase of oxoglutaric acid levels compared with control group.
            Succinic acid Click to Show/Hide the Full List of Regulating Pair(s):   1 Pair(s)
               Detailed Information Metabo  Info click to show the details of this metabolite
               Regulating Pair Experim Info click to show the details of experiment for validating this pair [1]
                      Introduced Variation Knockout of OGDH
                      Induced Change Succinic acid concentration: decrease
                      Summary Introduced Variation         Induced Change 
                      Disease Status Cervical Cancer [ICD-11: 2C77]
                      Details It is reported that knockout of OGDH leads to the decrease of succinic acid levels compared with control group.
References
1 Mitochondrial Protein Lipoylation and the 2-Oxoglutarate Dehydrogenase Complex Controls HIF1 Stability in Aerobic Conditions. Cell Metab. 2016 Nov 8;24(5):740-752.

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