Q0CJ57 · ATE_ASPTN

Function

function

Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of terreic acid, a quinone epoxide inhibitor of Bruton's tyrosine kinase (PubMed:24534845, PubMed:25265334).
The first step of the pathway is the synthesis of 6-methylsalicylic acid (6-MSA) by the 6-methylsalicylic acid synthase atX (PubMed:25265334, PubMed:9003280, PubMed:9438344).
In the biosynthesis of 6-MSA, atX utilizes one acetyl-CoA and three malonyl-CoAs as its substrates and catalyzes a series of programmed reactions including Claisen condensation, dehydration, reduction, and cyclization to yield 6-MSA (PubMed:25265334, PubMed:9003280, PubMed:9438344).
The 6-methylsalicylic acid decarboxylase atA then catalyzes the decarboxylative hydroxylation of 6-MSA to 3-methylcatechol (PubMed:25265334).
The next step is the conversion of 3-methylcatechol to terremutin via several oxidation steps involving the cytochrome P450 monooxygenase atE and probably also the cytochrome P450 monooxygenase atG (PubMed:25265334).
Lastly, atC is required for the oxidation of terremutin to terreic acid (PubMed:25265334).
No function could be assigned to atD yet, although it is involved in the biosynthesis of terreic acid (PubMed:25265334).

Cofactor

heme (UniProtKB | Rhea| CHEBI:30413 )

Biotechnology

Terreic acid is a metabolite with antibiotic properties (PubMed:23686727).
Terric acid acts also as a selective inhibitor of human Bruton's tyrosine kinase in mast cells and other immune cells (PubMed:10051623).

Pathway

Secondary metabolite biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site387Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue

GO annotations

AspectTerm
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 atE
  • EC number
  • Alternative names
    • Terreic acid biosynthesis cluster protein E

Gene names

    • Name
      atE
    • ORF names
      ATEG_06277

Organism names

Accessions

  • Primary accession
    Q0CJ57

Proteomes

Organism-specific databases

Phenotypes & Variants

Disruption phenotype

Abolishes the production of terreic acid, but accumulates (2Z,4E)-2-methyl-2,4-hexadienedioic acid, a degradation product of 3-methylcatechol (PubMed:25265334).

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004376391-467Cytochrome P450 monooxygenase atE

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the cytochrome P450 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    467
  • Mass (Da)
    53,877
  • Last updated
    2006-10-17 v1
  • Checksum
    98F88D661ABD5F3F
MSKWAKQYGGIFSLKRFRNTTIVLTDWKIMKELVDKKSTNFSHRPPSKVADLITRGNHILMMQYGETWRTMRKLIHQYLMESQCEKEHWKVQEAEAAQMLHDFLVDPENHMKHPKRYSNSITMSLVFGIRAKSVNDEYMTRLYSLMEKWSLVLETGATPPVDSWPLLQWIPERFMGYWRRRATEVGDLMTGLYTEVLHVIENRRKAGIYKDSLMDRVLDKKDKYRFDEHQLAFLGGTLMEGGSDTSSSLILAIVQAMTQYPEVQKKAHAEIDSVIGTDRSPAWSDFRKLPYINMMIKEAHRWRPVLPLGVVHGLATDDSYNGMHLPKHSTVILNVWGMHMDPDRFENPDAFIPERYANFPELAPHYAALADGAARDHFGYGAGRRICPGIHLAERNLFIAVAKLLWAFEFKNNPAGKNDASAETGSSQGFMHCVKDYDAIVTVRGEERRQTILRELEQAQTVFAKYD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CH476602
EMBL· GenBank· DDBJ
EAU32821.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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