A1CFL8 · PATK_ASPCL

Function

function

6-methylsalicylic acid synthase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (By similarity).
PatK catalyzes the first step of the pathway which is the synthesis of 6-methylsalicylic acid via condensation of 1 acetate and 3 malonate units (By similarity).
The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable) (PubMed:19383676).

Catalytic activity

Biotechnology

Patulin was originally used as an antibiotic and specifically trialed to be used against the common cold, but it is no longer used for that purpose since it has been shown to induce immunological, neurological and gastrointestinal effects (PubMed:15082620).
Genotoxic effects of patulin with dose-dependent increase in DNA strand breaks in brain, liver and kidneys have been detected in mice (PubMed:22222931).
However, more recently, it has been proposed that patulin might also have anti-tumor properties (PubMed:26619846).

Pathway

Mycotoxin biosynthesis; patulin biosynthesis.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site146For beta-ketoacyl synthase activity
Active site281For beta-ketoacyl synthase activity
Active site321For beta-ketoacyl synthase activity
Active site900Proton acceptor; for dehydratase activity
Active site1065Proton donor; for dehydratase activity

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Function3-oxoacyl-[acyl-carrier-protein] synthase activity
Molecular Function6-methylsalicylic acid synthase activity
Molecular Functionfatty acid synthase activity
Molecular Functionphosphopantetheine binding
Biological Processfatty acid biosynthetic process
Biological Processpatulin biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    6-methylcalicylic acide synthase
  • EC number
  • Short names
    6MSAS
  • Alternative names
    • Non-reducing polyketide synthase patK
    • Patulin synthesis protein K

Gene names

    • Name
      patK
    • ORF names
      ACLA_093660

Organism names

Accessions

  • Primary accession
    A1CFL8

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00004371111-17206-methylcalicylic acide synthase
Modified residue1678O-(pantetheine 4'-phosphoryl)serine

Keywords

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, domain, compositional bias.

Type
IDPosition(s)Description
Region1-31Disordered
Domain1-399Ketosynthase family 3 (KS3)
Compositional bias14-29Basic and acidic residues
Region509-823Malonyl-CoA:ACP transacylase (MAT) domain
Region868-987N-terminal hotdog fold
Region868-1139Dehydratase (DH) domain
Domain868-1144PKS/mFAS DH
Region1001-1144C-terminal hotdog fold
Region1148-1545Product template (PT) domain
Domain1644-1718Carrier

Domain

Multidomain protein; including a starter unit:ACP transacylase (SAT) that selects the starter unit; a ketosynthase (KS) that catalyzes repeated decarboxylative condensation to elongate the polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and transfers the extender unit malonyl-CoA; a product template (PT) domain that controls the immediate cyclization regioselectivity of the reactive polyketide backbone; and an acyl-carrier protein (ACP) that serves as the tether of the growing and completed polyketide via its phosphopantetheinyl arm (By similarity).

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,720
  • Mass (Da)
    185,005
  • Last updated
    2007-01-23 v1
  • Checksum
    828565A00E61ADB3
MDKQSASGEIPAMRWEPYHRRDPRNAKELSKTTSRGYFLDHLEDFDSQFFGISPKEAEQMDPQQRISLEVAWEALEDAGIPAKGLSGSDTAVFWGVNSDDYSKLVLEDLPNIEAWMGIGTAYCGIPNRISYHLNLMGPSTAVDAACASSLVAIHHGVQAIQLGESKIAIVGGVNALCGPGLTRVLDKAGAISSEGFCRSFDDEAKGYGRGEGAAAIILKNLSRAINDKDRILAVIKGSAVAQDGKTNGIMAPNAKAQQLVAQNALAVGNIDPLTVRYVEAHATSTPLGDPTEISAIAAVYGVGRDSQDPCFIGSIKPNIGHLEAGAGAMGFIKATLAIRKGILPPQANLNKLNSRIDWDKAGVKVVQEATKWPETDTIRRASICSYGYGGTVSHAVIEQFLPLSGLESLQTQSPDGPGVLLLSGPQQKRLSVQAETLRKWIAQDGRNHDLSSVLTTLATRRDHHDYRAAMVVESHDDAETALEALAKGADHPLVAQGRVLGTDIRKDVVWVFSGHGAQWTDMGKELLNNPVFYRAIQPLDELVQAEIGLSPIEMLLTGDFDSSDRVQILTYIMQIGISAVLKSNGVFPQAIIGHSVGEIAASVVAGALTPAEGALIVTRRAALYRRVMGQGGMILVNLPASQVEQELGQREDLVVAIESSPSSCVVAGDRDVVAQAAESFKERGVKTFTVKTDIAFHSPTLNGLIDPMLEALAEDLAPSTPTVRLFSTSLVDPRGQDLRDIHYWTNNMVNRVRLTSAVNAAVEEGYRIFLEVSSHPVVTHSINETLMDGGLEDFAVIPTLLRQKPTEKHILYSIAQLHCRGAEVDWKAQLPGPWADGLPTTTWMHKPIWRKIESAPLHTGLTHDVEKHTLLGQRIGIAGTNTTVYTTRLDNDTKPFPGSHPLHGTEIVPAAGLINTFMKGTGGRRLQNVVLRVPVAINAPRSVQVVVQEDQVKIMSRLLSDTPQATEDDSSWATHTTAYWARDIQEAVDPIDIAAVKKRLGTRIRDDFSINYLDQVGVSAMGFPWAITEHYHKDKEMIARVDVNPAVTGDAPLPWDSSSWAPILDAATSVGSTVFGTPALRMPAQIDRVDIFTSQDPPKIGWLYVEDASDAAPTSHVSVLNEAGEVVAKFTAMRFSEIEGTPGVSGSMESLVHQLAWPPATPAEEPLSIDTVLLVSSDAATMRQYANTIPRGVRSFEFSSVQDLISQDKSGLRLDKGTAVAYIPGEVQSLEEIPAASESFTWEVLELVKYIVKGGLPLKAFILTSNVGSGETPTALAQAPLFGLARIIASEHPDLGCLIDSENPVFPLTAMRYIQGADVIRINDDVARTARLRSLPRNKLHPASQPPRLLPRSEGTYLITGGLGVLGLETADFLVENGARRLILISRRALPPRRTWDAAPSDLQPTLAKIRNLESRGATVHILPLDISHPAAATQLSTALDTLSLPPVLGVVHAAGVLDNQLILETTRDAFTRVLAPKIAGALALHAVFPPNTLDFFLLFSSCGNLFGFPGQASYGAGNAFLDTLATHRARLGDAAVAVQWTSWRGMGMGASTEFINAELESKGITDVTRDEAFGAWLHLARYDIDHGVVLRSLAFDEGEPLPVSILTDIAVRRVGVAAAGDVPGTAAAGGADAIPSSGPELKVYLDEKIRGCVAKVLQMGAEDVDSKAALADLGVDSVMTVSLRRQLQQTLKVKVPSTLTWSHPTVSHLVGWFAEKVGK

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias14-29Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DS027052
EMBL· GenBank· DDBJ
EAW11667.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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