Q73WX4 · KGD_MYCPA

Function

function

Shows three enzymatic activities that share a first common step, the attack of thiamine-PP on 2-oxoglutarate (alpha-ketoglutarate, KG), leading to the formation of an enamine-thiamine-PP intermediate upon decarboxylation. Thus, displays KGD activity, catalyzing the decarboxylation from five-carbon 2-oxoglutarate to four-carbon succinate semialdehyde (SSA). Also catalyzes C-C bond formation between the activated aldehyde formed after decarboxylation of alpha-ketoglutarate and the carbonyl of glyoxylate (GLX), to yield 2-hydroxy-3-oxoadipate (HOA), which spontaneously decarboxylates to form 5-hydroxylevulinate (HLA). And is also a component of the 2-oxoglutarate dehydrogenase (ODH) complex, that catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. The KG decarboxylase and KG dehydrogenase reactions provide two alternative, tightly regulated, pathways connecting the oxidative and reductive branches of the TCA cycle (By similarity).

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

thiamine diphosphate (UniProtKB | Rhea| CHEBI:58937 )

Activity regulation

Alpha-ketoglutarate dehydrogenase and decarboxylase activities are inhibited by unphosphorylated GarA, and allosterically activated by acetyl-CoA, the main substrate of the TCA cycle.

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; succinate from 2-oxoglutarate (transferase route): step 1/2.
Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-CoA from 2-oxoglutarate (dehydrogenase route): step 1/1.

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site332Proton acceptor; for succinyltransferase activity
Binding site558thiamine diphosphate (UniProtKB | ChEBI)
Binding site5972-oxoglutarate (UniProtKB | ChEBI)
Binding site6222-oxoglutarate (UniProtKB | ChEBI)
Binding site622thiamine diphosphate (UniProtKB | ChEBI)
Binding site624thiamine diphosphate (UniProtKB | ChEBI)
Binding site665Mg2+ (UniProtKB | ChEBI)
Binding site665thiamine diphosphate (UniProtKB | ChEBI)
Binding site666thiamine diphosphate (UniProtKB | ChEBI)
Binding site667thiamine diphosphate (UniProtKB | ChEBI)
Binding site698Mg2+ (UniProtKB | ChEBI)
Binding site698thiamine diphosphate (UniProtKB | ChEBI)
Binding site700Mg2+ (UniProtKB | ChEBI)
Binding site10402-oxoglutarate (UniProtKB | ChEBI)
Binding site1058acetyl-CoA (UniProtKB | ChEBI); allosteric activator
Binding site1074acetyl-CoA (UniProtKB | ChEBI); allosteric activator
Binding site1109acetyl-CoA (UniProtKB | ChEBI); allosteric activator
Binding site1112acetyl-CoA (UniProtKB | ChEBI); allosteric activator
Binding site1162acetyl-CoA (UniProtKB | ChEBI); allosteric activator
Binding site1169acetyl-CoA (UniProtKB | ChEBI); allosteric activator
Binding site1170acetyl-CoA (UniProtKB | ChEBI); allosteric activator

GO annotations

AspectTerm
Molecular Function2-hydroxy-3-oxoadipate synthase activity
Molecular Function2-oxoglutarate decarboxylase activity
Molecular Functiondihydrolipoyllysine-residue succinyltransferase activity
Molecular Functionmagnesium ion binding
Molecular Functionoxoglutarate dehydrogenase (succinyl-transferring) activity
Molecular Functionthiamine pyrophosphate binding
Biological Processtricarboxylic acid cycle

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Multifunctional 2-oxoglutarate metabolism enzyme
  • Alternative names
    • 2-hydroxy-3-oxoadipate synthase (HOA synthase; HOAS) (EC:2.2.1.5) . EC:2.2.1.5 (UniProtKB | ENZYME | Rhea)
    • 2-oxoglutarate carboxy-lyase
    • 2-oxoglutarate decarboxylase
    • Alpha-ketoglutarate decarboxylase (KG decarboxylase; KGD) (EC:4.1.1.71) . EC:4.1.1.71 (UniProtKB | ENZYME | Rhea)
    • Alpha-ketoglutarate-glyoxylate carboligase

Including 2 domains:

  • Recommended name
    2-oxoglutarate dehydrogenase E1 component
  • EC number
  • Short names
    ODH E1 component
  • Alternative names
    • Alpha-ketoglutarate dehydrogenase E1 component (KDH E1 component)
  • Recommended name
    Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
  • EC number
  • Alternative names
    • 2-oxoglutarate dehydrogenase complex E2 component (ODH E2 component; OGDC-E2)
    • Dihydrolipoamide succinyltransferase

Gene names

    • Name
      kgd
    • Ordered locus names
      MAP_2536

Organism names

Accessions

  • Primary accession
    Q73WX4

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003107171-1247Multifunctional 2-oxoglutarate metabolism enzyme

Interaction

Subunit

Homodimer. The 2-oxoglutarate dehydrogenase (ODH) complex contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, coiled coil.

TypeIDPosition(s)Description
Region1-412-oxoglutarate dehydrogenase E1, N-terminal part
Region23-118Disordered
Region42-104Linker
Region105-353Succinyltransferase E2
Region354-12472-oxoglutarate dehydrogenase E1, C-terminal part
Coiled coil803-833

Domain

Is a fusion protein with two major domains exhibiting structural features of an E1 and E2 protein, and a short sequence stretch of E1 localized at the N-terminus, which is connected by a linker region to the rest of the protein.

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,247
  • Mass (Da)
    137,073
  • Last updated
    2004-07-05 v1
  • Checksum
    D31E9876D146519A
MSNISSPFGQNEWLVEEMYRKFRDDPSSVDPSWHEFLVDYNPEPTGDSVLAAPASTDGPSAPAPAAPQTAQPALPAQTAPPAQTAQPARPAPQPAAAPGNGASTRPAKPATPPPAEGDELQTLRGAAAAVVKNMSASLEVPTATSVRAIPAKLLIDNRIVINNQLKRTRGGKISFTHLLGYALVQAIKKFPNMNRHYAEIDGKPTAITPAHTNLGLAIDLQGKDGKRSLVVAGIKNCETMRFAQFVTAYEDIVRRARDGKLTAEDFAGVTISLTNPGTIGTVHSVPRLMNGQGAIIGVGAMEYPAEFQGASEERIAELGIGKLITLTSTYDHRIIQGAESGDFLRTIHEMLLSDGFWDDIFRELSIPYLPIRWSTDNPDSIVDKNARVMELIAAYRNRGHLMADIDPLRLDGSRFRSHPDLEILNHGLTLWDLDRVFKVNGFAGAEYKKLRDILGLLRDAYCRHIGVEYTHILDPEQQEWLQQRVETKHVKPTVAEQKFILSKLNAAEAFETFLQTKYVGQKRFSLEGAESVIPMMDAAIDQCAEHGLDEVVIGMPHRGRLNVLANIVGKPYSQIFSEFEGNLNPAQAHGSGDVKYHLGATGVYLQMFGDNDIQVSLTANPSHLEAVDPVLEGLVRAKQDLLDHGADDQGDEKAFSVVPMMLHGDAAFAGQGVVAETLNLTHLPGYRVGGTIHIIVNNQIGFTTAPEHSRSSEYCTDVAKMIGAPIFHVNGDDPEACAWVAKLAVDFRQKFKKDVVIDMLCYRKRGHNEGDDPSMTNPAMYDVVDIKRGVRKSYTEALIGRGDISMKEAEDALRDYQGQLERVFNEVRELEKHGVGPSESVEADQMLPAGLATAVDKALLARIGDAFLALPEGFTAHPRVQPVLEKRREMAYEGKIDWAFAELLALGSLVAGGKLVRLSGQDTRRGTFSQRHSVIIDRNTGEEFTPLQLLATNPDGTPTGGKFLVYDSPLSEYAAVGFEYGYTVGNPDALVLWEAQFGDFVNGAQSIIDEFISSGEAKWGQLSNVVLLLPHGHEGQGPDHTSARIERFLQLWAEGSMTIAMPSTPSNYFHLLRRHALDGIKRPLIVFTPKSMLRNKAAVSDIKDFTEIKFRSVLEEPTYEDGIGDRGKVSRVLLTSGKLYYELVARKNKDNRDDVAIVRIEQLAPLPKRRLGETLDRYPNVREYFWVQEEPANQGAWPRFGLELPELLPDKLTGLKRISRRAMSAPSSGSSKVHAVEQQEIIDTAFA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE016958
EMBL· GenBank· DDBJ
AAS04853.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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