OGDH
entrez
4967
canonical
uniprot
Q02218
canonical
ensembl
ENSG00000105953
resolver
ensp
ENSP00000222673
resolver
ensp
ENSP00000388084
resolver
ensp
ENSP00000388183
resolver
ensp
ENSP00000392878
resolver
ensp
ENSP00000414662
resolver
ensp
ENSP00000576429
resolver
ensp
ENSP00000576432
resolver
ensp
ENSP00000576437
resolver
ensp
ENSP00000576446
resolver
ensp
ENSP00000576455
resolver
ensp
ENSP00000576458
resolver
enst
ENST00000444676
resolver
enst
ENST00000447398
resolver
enst
ENST00000906378
resolver
enst
ENST00000906387
resolver
enst
ENST00000906396
resolver
enst
ENST00000906399
resolver
genesymbol
OGDH
resolver
hgnc
HGNC:8124
resolver
uniprot
A0A140VJQ5
resolver
uniprot
B4DH65
resolver
uniprot
B4E2U9
resolver
uniprot
B4E3E9
resolver
uniprot
D3DVL0
resolver
uniprot
E9PBM1
resolver
uniprot
E9PCR7
resolver
uniprot
E9PDF2
resolver
uniprot
Q96DD3
resolver
uniprot
Q9UDX0
resolver
uniprot_entry
A0A140VJQ5_HUMAN
resolver
uniprot_entry
B4DH65_HUMAN
resolver
uniprot_entry
B4E3E9_HUMAN
resolver
uniprot_entry
E9PCR7_HUMAN
resolver
uniprot_entry
E9PDF2_HUMAN
resolver
uniprot_entry
ODO1_HUMAN
resolver
uniprot_sec
B4E2U9
resolver
uniprot_sec
D3DVL0
resolver
uniprot_sec
E9PBM1
resolver
uniprot_sec
Q96DD3
resolver
uniprot_sec
Q9UDX0
resolver
activity_regulation
ACTIVITY REGULATION: Calcium ions and ADP stimulate, whereas ATP and NADH reduce catalytic activity. {ECO:0000269|PubMed:24495017}.
uniprot
proteins
amino_acid_sequence
MFHLRTCAAKLRPLTASQTVKTFSQNRPAAARTFQQIRCYSAPVAAEPFLSGTSSNYVEEMYCAWLENPKSVHKSWDIFFRNTNAGAPPGTAYQSPLPLSRGSLAAVAHAQSLVEAQPNVDKLVEDHLAVQSLIRAYQIRGHHVAQLDPLGILDADLDSSVPADIISSTDKLGFYGLDESDLDKVFHLPTTTFIGGQESALPLREIIRRLEMAYCQHIGVEFMFINDLEQCQWIRQKFETPGIMQFTNEEKRTLLARLVRSTRFEEFLQRKWSSEKRFGLEGCEVLIPALKTIIDKSSENGVDYVIMGMPHRGRLNVLANVIRKELEQIFCQFDSKLEAADEGSGDVKYHLGMYHRRINRVTDRNITLSLVANPSHLEAADPVVMGKTKAEQFYCGDTEGKKVMSILLHGDAAFAGQGIVYETFHLSDLPSYTTHGTVHVVVNNQIGFTTDPRMARSSPYPTDVARVVNAPIFHVNSDDPEAVMYVCKVAAEWRSTFHKDVVVDLVCYRRNGHNEMDEPMFTQPLMYKQIRKQKPVLQKYAELLVSQGVVNQPEYEEEISKYDKICEEAFARSKDEKILHIKHWLDSPWPGFFTLDGQPRSMSCPSTGLTEDILTHIGNVASSVPVENFTIHGGLSRILKTRGEMVKNRTVDWALAEYMAFGSLLKEGIHIRLSGQDVERGTFSHRHHVLHDQNVDKRTCIPMNHLWPNQAPYTVCNSSLSEYGVLGFELGFAMASPNALVLWEAQFGDFHNTAQCIIDQFICPGQAKWVRQNGIVLLLPHGMEGMGPEHSSARPERFLQMCNDDPDVLPDLKEANFDINQLYDCNWVVVNCSTPGNFFHVLRRQILLPFRKPLIIFTPKSLLRHPEARSSFDEMLPGTHFQRVIPEDGPAAQNPENVKRLLFCTGKVYYDLTRERKARDMVGQVAITRIEQLSPFPFDLLLKEVQKYPNAELAWCQEEHKNQGYYDYVKPRLRTTISRAKPVWYAGRDPAAAPATGNKKTHLTELQRLLDTAFDLDVFKNFS
uniprot
proteins
ec_number
1.2.4.2
uniprot
proteins
function
FUNCTION: 2-oxoglutarate dehydrogenase (E1o) component of the 2-oxoglutarate dehydrogenase complex (OGDHC) (PubMed:24495017, PubMed:25210035, PubMed:28435050). Participates in the first step, rate limiting for the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2) catalyzed by the whole OGDHC (PubMed:24495017, PubMed:25210035, PubMed:28435050). Catalyzes the irreversible decarboxylation of 2-oxoglutarate (alpha-ketoglutarate) via the thiamine diphosphate (ThDP) cofactor and subsequent transfer of the decarboxylated acyl intermediate on an oxidized dihydrolipoyl group that is covalently amidated to the E2 enzyme (dihydrolipoyllysine-residue succinyltransferase or DLST) (PubMed:24495017, PubMed:25210035, PubMed:28435050, PubMed:35272141). Plays a key role in the Krebs (citric acid) cycle, which is a common pathway for oxidation of fuel molecules, including carbohydrates, fatty acids, and amino acids (PubMed:25210035). Can catalyze the decarboxylation of 2-oxoadipate in vitro, but at a much lower rate than 2-oxoglutarate (PubMed:28435050). Can also convert 2-keto-4-hydroxyglutarate (KHG) and CoA into malyl-CoA (By similarity). Mainly active in the mitochondrion (PubMed:29211711). 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 (PubMed:29211711). {ECO:0000250|UniProtKB:K9IVI1, ECO:0000269|PubMed:24495017, ECO:0000269|PubMed:25210035, ECO:0000269|PubMed:28435050, ECO:0000269|PubMed:29211711, ECO:0000303|PubMed:25210035}.
uniprot
proteins
mass_dalton
115935
uniprot
proteins
mutagenesis
MUTAGEN 154; /note="D->A: Six-fold decrease in sensitivity for calcium."; /evidence="ECO:0000269|PubMed:24495017"; MUTAGEN 459..460; /note="PY->AA: Abolished enzyme activity and ability to promote histone succinylation."; /evidence="ECO:0000269|PubMed:29211711
uniprot
proteins
protein_family
Alpha-ketoglutarate dehydrogenase family
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
1542694
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17370265
uniprot
proteins
pubmed
18973345
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24495017
uniprot
proteins
pubmed
25210035
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
28435050
uniprot
proteins
pubmed
29211711
uniprot
proteins
pubmed
32792488
uniprot
proteins
pubmed
35272141
uniprot
proteins
pubmed
7622061
uniprot
proteins
sequence_length
1023
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:29211711}. Nucleus {ECO:0000269|PubMed:29211711}. Note=Mainly localizes in the mitochondrion. A small fraction localizes to the nucleus, where the 2-oxoglutarate dehydrogenase complex is required for histone succinylation. {ECO:0000269|PubMed:29211711}.
uniprot
proteins