A0A4P8WAD3 · PYIA_PYRGI

Function

function

O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology (Probable) (PubMed:31099577).
Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass (PubMed:31099577).
The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine (PubMed:31099577).
The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone (PubMed:31099577).
The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor (PubMed:31099577).
As the NRPS A-domain demonstrates substrate tolerance, pyiS can also use phenylalanine, tyrosine and even para-chlorophenylalanine as amino acid precursor, which leads to the production of novel cytochalasans, including halogenated cytochalasans (PubMed:31099577).
Because pyiS lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase pyiC (PubMed:31099577).
Reduction by the hydrolyase pyiE leads to 1,5-dihydropyrrolone, which is substrate for dehydration and intra-molecular Diels-Alder cyclization by the Diels-Alderase pyiF to yield the required isoindolone-fused macrocycle (PubMed:32039410).
The tailoring cytochrome P450 monooxygenases piyD and piyG catalyze the hydroxylation at C-18 and C-7, respectivily, whereas the short-chain dehydrogenase/reductase pyiH reduces the carbonyl at C-21 in preparation for the transfer of an acetyl group by the acetyltransferase pyiB (PubMed:31099577).
These 3 reactions whose order is not clear yet, lead to the production of O-methylpyrichalasin J, a deacetylated pyrichalasin H (PubMed:31099577).
Finally, pyiB to converts O-methylpyrichalasin J into the final product pyrichalasin H via acetylation of C-21 (PubMed:31099577).

Pathway

Mycotoxin biosynthesis.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site271S-adenosyl-L-methionine (UniProtKB | ChEBI)
Active site317Proton acceptor

GO annotations

AspectTerm
Molecular FunctionO-methyltransferase activity
Biological Processmethylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    O-methyltransferase pyiA
  • EC number
  • Alternative names
    • Pyrichalasin H biosynthesis cluster protein A

Gene names

    • Name
      pyiA

Organism names

Accessions

  • Primary accession
    A0A4P8WAD3

Proteomes

Phenotypes & Variants

Disruption phenotype

Leads to the loss of pyrichalasin H production, but accumulates the tyrosine and phenylalanine analogs of pyrichalasin H, called magnachalasin H and cytochalasin H.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004494511-409O-methyltransferase pyiA

Family & Domains

Features

Showing features for compositional bias, region.

TypeIDPosition(s)Description
Compositional bias1-43Polar residues
Region1-46Disordered

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    409
  • Mass (Da)
    45,694
  • Last updated
    2019-07-31 v1
  • Checksum
    9FB375240610AC9E
MASQDGTTELLSQSVNSTCIPGSTYHVDRGRASSASTPPTSPPLSEVDYTPLLESTQEPRHEYTQLAHSLVKAMADYVGHLQEENLPMPSLEPAAQVHGGLKVQGGVAARDTVVKLAQKIVAMTMDPEMKLFISSLQFHFCSSLKVAIDLRVHELDECFRASSRQADALALARYREPHEADTLGFGLAFNTTANFWEVLARDTEGKRSQRFNRAMRAVNINALEVIPRIYPFNRIGGNGLLVDVGGGLGQVARAIMATNQGSRLQRCIVQDVCAADDVLEEVLESNRKLGVELQRHDFFDKQPVTGASIYFFRHIFHDWPDRACVKILKQIVQAMGRDSRLLICDQVVDDEPSIPATLYDIDMWTLFGGKERNRSEWEALFRAADERLYIKKVWTTTEAPTTILEVCLW

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-43Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MK801691
EMBL· GenBank· DDBJ
QCS37511.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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