V5Y0F7 · AF161_ALTAL

Function

function

Reducing polyketide synthase; part of the gene clusters that mediate the biosynthesis of the host-selective toxins (HSTs) AF-toxins responsible for Alternaria black spot of strawberry disease by the strawberry pathotype (Probable). AF-toxin I and III are valine derivatives of 2,3-dyhydroxy-isovaleric acid and 2-hydroxy-isovaleric acid respectively, while AF II is an isoleucine derivative of 2-hydroxy-valeric acid (PubMed:15066029, PubMed:22846083, Ref.4). These derivatives are bound to a 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid (EDA) moiety (PubMed:15066029, PubMed:22846083, Ref.4). On cellular level, AF-toxins affect plasma membrane of susceptible cells and cause a sudden increase in loss of K+ after a few minutes of toxin treatment (PubMed:22846083).
The aldo-keto reductase AFTS1 catalyzes the conversion of 2-keto-isovaleric acid (2-KIV) to 2-hydroxy-isovaleric acid (2-HIV) by reduction of its ketone to an alcohol (PubMed:15066029).
The acyl-CoA ligase AFT1, the hydrolase AFT2 and the enoyl-CoA hydratases AFT3 and AFT6, but also the polyketide synthase AFT9, the acyl-CoA dehydrogenase AFT10, the cytochrome P450 monooxygenase AFT11 and the oxidoreductase AFT12 are all involved in the biosynthesis of the AK-, AF- and ACT-toxin common EDA structural moiety (PubMed:12019223, PubMed:18986255, Ref.4). The exact function of each enzyme, and of additional enzymes identified within the AF-toxin clusters have still to be determined (PubMed:12019223, PubMed:18986255, Ref.4).

Miscellaneous

Gene clusters encoding host-selective toxins (HSTs) are localized on conditionally dispensable chromosomes (CDCs), also called supernumerary chromosomes, where they are present in multiple copies (PubMed:12019223).
The CDCs are not essential for saprophytic growth but controls host-selective pathogenicity (PubMed:12019223).

Pathway

Mycotoxin biosynthesis.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site194For beta-ketoacyl synthase activity
Active site333For beta-ketoacyl synthase activity
Active site382For beta-ketoacyl synthase activity
Active site990Proton acceptor; for dehydratase activity
Active site1170Proton donor; for dehydratase activity

GO annotations

AspectTerm
Molecular Function3-oxoacyl-[acyl-carrier-protein] synthase activity
Molecular Functionfatty acid synthase activity
Molecular Functionoxidoreductase 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
    Reducing polyketide synthase AFT16-1
  • EC number
  • Short names
    PKS AFT16-1
  • Alternative names
    • AF-toxin biosynthesis protein 16-1

Gene names

    • Name
      AFT16-1

Organism names

Accessions

  • Primary accession
    V5Y0F7

Organism-specific databases

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00004448541-2349Reducing polyketide synthase AFT16-1
Modified residue2307O-(pantetheine 4'-phosphoryl)serine

Keywords

Structure

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-21Disordered
Domain20-462Ketosynthase family 3 (KS3)
Region37-80Disordered
Region578-888Malonyl-CoA:ACP transacylase (MAT) domain
Region958-1092N-terminal hotdog fold
Region958-1263Dehydratase (DH) domain
Domain958-1269PKS/mFAS DH
Region1111-1269C-terminal hotdog fold
Region1976-2164Ketoreductase (KR) domain
Domain2273-2347Carrier

Domain

Multidomain protein; including 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 dehydratase (DH) domain that reduces hydroxyl groups to enoyl groups; a ketoreductase (KR) domain that catalyzes beta-ketoreduction steps; and an acyl-carrier protein (ACP) that serves as the tether of the growing and completed polyketide via its phosphopantetheinyl arm.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    2,349
  • Mass (Da)
    257,802
  • Last updated
    2014-02-19 v1
  • MD5 Checksum
    B782292165F4CC5217845DCA5D94DECA
MNGKSRDNGHDGKRQPVVPAEPIAIVGTAMRLPGDATNPSKLWQLLRNPPSDLSRRPPSERFSSAGFFHEDPEHHGTSNSEQSYFLREDIRAFDAAFFSIAPREAEAIDPQHRLLLEVVYEALEAAGIPLEKTQGSDTAVYVGQMSNDYWDHLLRDLDSIPKYMATGTARSVTANRLSYFFDWHGPSMTIDTACSSSMVALHEAVQVLRSGRAGMAVAAGCHLVLGPESYVIESKLRMISPTGTCKMWDAGADGYARAEGCAALILKTLSSALRDGDPIAALIRETGVNQDGRTRGITMPSAQAQAALIRETYLRAGLDPTHPRDQPQLFEAHGTGTQAGDPIEAEAIHLAFFNDGVAHKGTRERKEREKLLVGSIKTVVGHLEATAGLAGILKGIAAMNHRMVPPNLWFRTLNQRIAPFYRDFRVPTVLEEWPMTGFDGTLRCSVNSFGFGGTNAHTILESYEPQLVTATKMPREISFITPLTFSAASAASLVAVVDSYRRHLASKQDISLADLAFTLQSRRSALPYRIAFSGTDITSLIKQMSESVDSVKGTANVSIGTLNQQGKLEGGPPKLLGVFTGQGAQWPGMGRELLKSSKVFSDAIIKMEDSLATLPDPPSWSLVDQFKAKASPSSSEEATVAQPVSLALQIGLVDLLRASGVEFDSVVAHSSGEIAAAYTTGLISAHDAIRIAYYRGKYSALATEGGGMMAVGMSFAEAEAFCNQEQLRGRVTAAASNSPKSTTLSGRLSTLKEAASLLGNTFHRFLKVDKAYHSDAMLPCCKPFQAILEKCDIKVHKPNDVLWVSSVREGQQPRSFADLLSGPYWVETLHKPVLFSQALTRVLQMRSFDATLEIGPHPALRGPSLQTHADISLEKGKVLLYKGVLERFKHDGEAFSSCLGFLWQHFGWAHFEAYRSTSLTTDVPRVLDQLPTYPWNHESLYWTESSNSYRFRYREAYHPLLGFRSVDSHAMELRWKNVWSLREMPWLKGHVVQGQAVVPGVSYVTLALEAAAALGREGQETTRIELHDINIHRAIIVEEDEYSGTNVFVSVSRQNPDASCTRATFNIYASTNHEKEPFHVCSGDILLSHFAKDSGIQALGEFVVSTVYKDMSSVEPSLFYSEMKEVGLCWKEPFLSDSMYRSHHRSVLSATRSTADAHDGQLLLSPVLLDIGFQGALVGFASPGDGRLWNPYLPTHIDRCTFDLENLKLNKPCYDEVYFSSAVMGSTLPDLSTTATFTCDVYGFYAIDGNPFVQVEGLKFSCMYPAQETNDREMFANETWMPASPLDMELQPYDAQKHMGNLGAVVENLSHCDPRMKILHISDGESLVVPILESLQGAFARLDIADSSQSPALRHVEEVKELFPKDSKRIWSSDLNLTKLTSSPAIAENSYDLIICAQTIETGDDVESRCSKLRKLLKLGGSIILSTSPGTSCNLPLQRCGFTGVELELSVGPESRLILTRAKDDTSKTLETPLDDLDACTGEVIVIGGHQPEIQAIVDTFQKDVAGKLSKMTLLESLSDLETYGIPTDATVLCLADLHDDTLRNLAEGTLGGMKLLFETARRVLWVTQGRRNQNPFASMMVGLGRCIISESPLLNLQFLDIEDPLSDPVTHKTISECFIRLISLTTTGDFNVVRSWNQEPEMVLSQGKLLIPRIRPLPALNDRLNCQNRIIKKPLIAGDGTSVELTRSGAFYAAQEYDDYSAGRRITISHSVSLPIELPGQMKGYLGLGTMSSGERVVVISPNNRNIQSAEECAFAVHFQPRGNEADTLALIASAIFIRMAWEHTSDYVVLHQPSQSVYRLGTQMAEDAKSKLYFSVSGRNDLEKHANVVSIPSMATRQSLRNLMPGQVGAFIHVPGLAGAGDRVSADRMIRAMSTTCKIFHLATAAASSQNKSIDIRLSFNWKKACRILVQSVEDVAKFGNSNMLAENQPVKCIGIAEISGTPFSYDAARIIDWTKDSRLKVNIQSKNPTKHFSPNKTYLLVGLTGDLGRSLAQWMVRCGAQHIVLTSRSPRVPDSWLQACREISPQAQVRVFKMDVTDEADVRSVCHSICKSMPPIGGVANAAMVMDDCLFHKLQLASFNRVVEPKVVGSMILDKIFHDVDLDFFIMFSSISCIVGNRGQSSYSAANLAETTIASGRRSRGLSASTLALGMVVGVGYVARANLPTEAIKDNVRMQNGIPLGETDVHTAFFEAMLLGKESSRLIPELITGLKSIGSEDVELPLWHENPRFSHLSLLEGLDDVSLDSKKSSQGKVSVREQLRQSTMPQEPFEILSGSLKQKLKVMLKIDKQEISDEVALVQMGIDSLSAVEIRSWFAKEVGVDLPVLKILNGASIRGLCLEAIGQWKK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB872925
EMBL· GenBank· DDBJ
BAO10621.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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