A0A1L9WN37 · ACUA_ASPA1

Function

function

6-methylsalicylic acid synthase; part of the gene cluster that mediates the biosynthesis of aculins (PubMed:26374386).
The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) acuA via condensation of acetate and malonate units (PubMed:26374386).
The 6-methylsalicylic acid decarboxylase acuB then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol) (Probable). These first reactions occur in the cytosol (By similarity).
The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase acuC converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase acuD (Probable). Gentisyl alcohol is further oxidized by the oxidoreductase acuE that probably catalyzes hydroxylation of the aromatic ring (Probable). The aromatic system might then be opened by oxidation through a Baeyer-Villiger type of oxidation, which could be catalyzed by acuF, with the carboxylic acid at C-1 subsequently reduced to an aldehyde by acuG (Probable). Subsequently, a hemiacetal is formed, before the dehydrogenase acuH would reduce the double bond between C-4 and C-6 (Probable). Finally, keto-enol tautomerism results in formation of aculinic acid, which exists as two diastereomers (both R/S configurations at C-1) by non-enzymatic hemiacetal formation (Probable). The carboxypeptidase acuI could be involved in the linking of aculinic acid to an aculene A moiety produced by the aculene biosynthesis cluster and which leads to the production of aculin A (Probable). AcuI may also be involved in the attachment of proline to aculinic acid to form epi-aculins A and B (Probable)

Catalytic activity

Pathway

Secondary metabolite biosynthesis.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site165For beta-ketoacyl synthase activity
Active site300For beta-ketoacyl synthase activity
Active site340For beta-ketoacyl synthase activity
Active site920Proton acceptor; for dehydratase activity
Active site1085Proton 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 Processsecondary metabolite biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    6-methylsalicylic acid synthase acuA
  • EC number
  • Short names
    6MSAS
  • Alternative names
    • Aculin biosynthesis cluster protein A
    • Non-reducing polyketide synthase acuA

Gene names

    • Name
      acuA
    • ORF names
      ASPACDRAFT_1904397

Organism names

Accessions

  • Primary accession
    A0A1L9WN37

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00004504121-17496-methylsalicylic acid synthase acuA
Modified residue1706O-(pantetheine 4'-phosphoryl)serine

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain1-418Ketosynthase family 3 (KS3)
Region528-843Malonyl-CoA:ACP transacylase (MAT) domain
Region888-1006N-terminal hotdog fold
Region888-1160Dehydratase (DH) domain
Domain888-1165PKS/mFAS DH
Region1021-1165C-terminal hotdog fold
Region1169-1629Product template (PT) domain
Domain1671-1746Carrier

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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,749
  • Mass (Da)
    187,960
  • Last updated
    2017-03-15 v1
  • Checksum
    E8001C481487766A
MACRVAGNNNNPEQLWQSLLQKKDASGEIPEMRWEPYLRRDSRNAKILKETTSRGYFLDRLEDFDGQFFGISPKEAEQMDPQQRLSLEVTWEALENAGITARSLSGSDTAVFWGVNSDDYSKLVLEDLPNVEAWMGIGTAYCGVPNRISYHLNLMGPSTAVDAACASSLVAVHHGVQAIILGESKVAIVGGVNALCGPGLTRVLDKAGAVSSEGRCCSFDNDVKGYGRGEGAAAIVLKNLSAAIKDGDHIMAVIKGTAVAQDGKTNGIMAPNAKAQQLVAHNALKVGNIDPLTVGYVEAHATSTPLGDPTEVSAIAAVYGADREPEAPCFIGSIKPNIGHLEAGAGAMGFIKAVMAVQKGVLAPQANLTTLTKKIDWDNVGLKVVQQETKWPATDDVRRAAICSYGYGGTVSHAVIEQFNFPETLDLKPGASATNPTVLLLSGPQEKRLPIQARALRNWLQADGSQQDLQRVAATLAVRRDHHDYRAAIVVESKEDAIQALGHLADGANDAWTSQSRVFGSGINRDVVWVFSGHGAQWADMGKELLQNPIFYQAVQPLDEIVEAEIGLSPIALLRSGEFEASDHVQILTYIMQIGISAVLHSHGVYPQAIIGHSVGEIAASVVAGALTAEEGAVLITRRSVLYRQVMGQGGMILVNKPYAEVAQELAGREDLVVAIDSSPSSCVVAGSTEAVAEKAAEFKERSIKTFTVRTDIAFHSPMLNQLVDPLMQSLEGSLAPTTPTRAKLYSTSLRDPRGSDLRDATYWANNMVNPVHLTSAVQAALDDSYRVFLEVSSHPLVSHSINETIMDAGIEDYCMIPTLARKKPSEKSILHAVGQLHTRGANVDWKSQLSGPWAGGLPNTSWMHKPTWRQIGAGPVSTSQTHDVEKHTLLGQRIGVAGTDTVVYTTRLDNESKPFPGSHPLHGTEIVPAAGLVNTFVKATGATVLNNVVLRVPVAINAPRSVQIVAQREDVKIMSRLIQENEGNNDDSSWVTHTTARWESSSSSPVPAQIDVEATKARIGTRLRDEFSIDYLDKVGVSAMGFPWAVTEHYGNTKEMIARVDAAPSVAADAELPWDASSWAPILDAATSVGSTIFFNEPRLRMPAQIERVDIFTRANPPKVGWLYVQEASDTALASHVSVCDEAGNVVAKFTSMRFSEIEGTPGVSGSMESLVHQMAWPPAVPAEEPLPINKLLLISQDVPLREAYAATISSSTQVTLLANANDLIINRAESLLTKETAIVYIPSQVSSLQDVPKSAETFTWQLLELIKFVVNNALPVKIFVVTSNTGEGETPTALAHAPLVGLSRVIASEHPDQFGGLIDTEVLTFPLTTMRYIQGADIIRIRDGVARTMRLRSLPRHRLIQQQDQQQQQPQLLPRPDGTYLITGGLGALGLEVADFLVTQGARRVILISRRGLPPRRLWSKMEPSSPLAPTITKILDLEARGATIHVLPLDISQLTAADALTTALDTLSLPPVRGVVHAAGVLDNELVLDTTPDAFARVLAPKITGGLVLNEVFPPQSVDFFILFSSCGQLVGFTGQSSYGAGNSFLDALASHRQARGDRGARAFQWTAWRALGMGASTDFINAELASKGITDVTADEAFAAWRHAARYEGIDHAVVLRALPLDADEPLPSPALADIIVRRSASASADSSPSSSPEKQTIPTSGPELKAYLDKAIRGCVAAVLHLPAADEVDSKAALADLGVDSVMTVTLRQKLQQALRVKVPPTLTWSHPTVGHLVGWFAEKVGKE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KV878982
EMBL· GenBank· DDBJ
OJJ97578.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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