Q2HEW1 · CHEG_CHAGB

Function

function

Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of chaetoglobosin A which has a unique inhibitory activity against actin polymerization in mammalian cells (PubMed:23611317, PubMed:33622536).
Chaetoglobosin A and its intermediates are involved in the morphological differentiation of C.globosum (PubMed:33622536).
The first step of the pathway is the synthesis of prochaetoglobosin I via condensation of one acetyl-CoA, 8 malonyl-CoA, and a L-tryptophan molecule by the PKS-NRPS hybrid synthetase cheA, followed by reduction of backbone double bond to install desired geometry by the enoyl reductase cheB (PubMed:23611317).
Further multiple oxidation steps performed by the cytochrome P450 monooxygenases cheE and cheG, as well as by the FAD-linked oxidoreductase cheF, lead to the formation of chaetoglobosin A (PubMed:23611317).
Depending on the order of action of these reductases, distinct intermediates can be identified (PubMed:23611317).
Within the pathway, the cytochrome P450 monooxygenase cheE catalyzes a stereospecific epoxidation on prochaetoglobosin I, cytoglobosin D, and chaetoglobosin J intermediates (PubMed:23611317).
The FAD-linked oxidoreductase cheF performs dehydrogenation of the C-20 hydroxyl groups in the 20-dihyrochaetoglobosin A and cytoglobosin D intermediates (PubMed:23611317).
Finally, the cytochrome P450 monooxygenase cheG can catalyze the stereospecific dihydroxylation of prochaetoglobosin I and prochaetoglobosin IV at C-19 and C-20, respectively (PubMed:23611317).
The Diels-Alderase cheD may play a role in the post-PKS-NRPS biosynthetic steps catalyzing Diels-Alder cyclization (Probable)

Cofactor

heme (UniProtKB | Rhea| CHEBI:30413 )

Pathway

Secondary metabolite biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site283Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue

GO annotations

AspectTerm
Cellular Componentmembrane
Molecular Functionheme binding
Molecular Functioniron ion binding
Molecular Functionmonooxygenase activity
Molecular Functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Cytochrome P450 monooxygenase cheG
  • EC number
  • Alternative names
    • Chaetoglobosin A biosynthesis cluster protein G

Gene names

    • Name
      cheG
    • ORF names
      CHGG_01243

Organism names

Accessions

  • Primary accession
    Q2HEW1

Proteomes

Organism-specific databases

Subcellular Location

Membrane
; Single-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane37-57Helical

Keywords

Phenotypes & Variants

Disruption phenotype

Impairs the production of chaetoglobosin A but leads to the accumulation of prochaetoglobosin IV (PubMed:23611317).

PTM/Processing

Features

Showing features for chain, glycosylation.

TypeIDPosition(s)Description
ChainPRO_00004382451-340Cytochrome P450 monooxygenase cheG
Glycosylation25N-linked (GlcNAc...) asparagine
Glycosylation322N-linked (GlcNAc...) asparagine

Keywords

PTM databases

Expression

Induction

Expression is positively regulated by the cluster-specific transcription factor cheR that binds directly to an asymmetric direct repeat present in the promoter.

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region308-340Disordered

Sequence similarities

Belongs to the cytochrome P450 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    340
  • Mass (Da)
    37,995
  • Last updated
    2006-03-21 v1
  • Checksum
    782A629292BF0FEF
MFPALQKIVVSTNASPLVGRELASNSTWIWHVERLPMLLGIPTVILSLTPAVLRLLIKPLLFVPIRYSSFVLTRLITPVLKEDMLEFESTADKKSPAGPKAKGKLALTSWLLSRYPASLKDRMSQLIRDYLAITFESTPSTSGVLFYILIELAAAPELAEAVRRELREVAPNGELPSTHLNELKVMDSVMRESARVNPFSHLVLYRKLLRPLKLEGCPELPAGCFICVDAHHIDFSPQLWENPERFDGLRHYRARQKPENGNRFKFANLGSDAPGWGDGPQACPGRMFADNTIKIILAHILTHYDLELPPGQGKPEKGSMPNGSMSPDTKAKVLFRSRKL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CH408029
EMBL· GenBank· DDBJ
EAQ93008.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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