S0DZM7 · BIK1_GIBF5

Function

function

Polyketide synthase; part of the gene cluster that mediates the biosynthesis of bikaverin, a red pigment also considered as a mycotoxin (PubMed:12409099, PubMed:17696354, PubMed:19400779).
The first stage is catalyzed by the polyketide synthase bik1, which catalyzes the formation of the intermediate SMA76a also knowm as pre-bikaverin (PubMed:12409099, PubMed:17696354, PubMed:19400779).
FAD-dependent monooxygenase bik2 might then be responsible for the oxidation of pre-bikaverin to oxo-pre-bikaverin which is in turn methylated by the O-methyltransferase bik3 to me-oxo-pre-bikaverin (PubMed:26382642).
A further cycle of oxydation and methylation by bik2 and bik3 leads to the final product of bikaverin, via a nor-bikaverin intermediate (PubMed:19400779, PubMed:26382642).

Pathway

Secondary metabolite biosynthesis.

Features

Showing features for active site.

120362004006008001,0001,2001,4001,6001,8002,000
TypeIDPosition(s)Description
Active site541For beta-ketoacyl synthase activity
Active site676For beta-ketoacyl synthase activity
Active site718For beta-ketoacyl synthase activity
Active site997For acyl/malonyl transferase activity
Active site1325Proton acceptor; for dehydratase activity
Active site1511Proton donor; for dehydratase activity
Active site1857For thioesterase activity

GO annotations

AspectTerm
Molecular Function3-oxoacyl-[acyl-carrier-protein] synthase activity
Molecular Functionfatty acid synthase activity
Molecular Functionphosphopantetheine binding
Biological Processfatty acid biosynthetic process
Biological Processphenol-containing compound biosynthetic process
Biological Processpolyketide biosynthetic process
Biological Processtoxin biosynthetic process

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Bikaverin polyketide synthase bik1
  • EC number
  • Alternative names
    • Bikaverin biosynthesis protein 1

Gene names

    • Name
      bik1
    • Synonyms
      pks4
    • ORF names
      FFUJ_06742

Organism names

Accessions

  • Primary accession
    S0DZM7

Proteomes

Organism-specific databases

Phenotypes & Variants

Disruption phenotype

Impairs the production of bikaverin and its intermediate oxo-pre-bikaverin (PubMed:12409099, PubMed:19400779, PubMed:26382642).

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00004363381-2036Bikaverin polyketide synthase bik1
Modified residue1690O-(pantetheine 4'-phosphoryl)serine

Keywords

Expression

Induction

Expression is repressed during the growth phase, but is induced as the growth rate decreases due to nitrogen depletion of the culture medium (PubMed:12409099).
Highly expressed only under acidic culture conditions (PubMed:12409099, PubMed:19400779).
Also induced by salt starvation (PubMed:19838698).
Expression is repressed by regulatory gene, areA, a transcriptional regulator responsible for the activation of nitrogen assimilation genes (PubMed:12409099).
Expression is also negatively regulated by vel1 (PubMed:20572938).

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, domain, compositional bias.

Type
IDPosition(s)Description
Region8-242N-terminal acylcarrier protein transacylase domain (SAT)
Domain370-801Ketosynthase family 3 (KS3)
Region908-1209Acyl/malonyl transferases
Region1293-1425N-terminal hotdog fold
Domain1293-1600PKS/mFAS DH
Region1295-1599Product template (PT) domain
Region1452-1600C-terminal hotdog fold
Region1628-1654Disordered
Compositional bias1629-1654Polar residues
Domain1653-1730Carrier
Compositional bias1733-1753Polar residues
Region1733-1758Disordered

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 back- bone; 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
    2,036
  • Mass (Da)
    221,460
  • Last updated
    2013-09-18 v1
  • Checksum
    FCA97D2EB05774D4
MASSADVYVFGDQSTPVLDKLQALVRVKDNALLTSFLGEAFLAVRREIVSLSSLERKSIPEAESLSLLLEGVRRSEPHAALDSAFVCIYEIGYYIDYLARSDKQHPPAAPSLLLGICTGSIAAAAVSCAKDVFEISRLGVEAATVAFRLGMHVRRRAENLGYSTPSSWSMILSSNQEELVSEALKEFSKEKNLTYSSRPYISATGPGFTTISGPPSILESVKSCDTFSGKRLYPAPIYGPYHNSSSYSESSLEHGLASILEDVGFLENEMLIPIISCASGSRLDQLSFGNLLKNVLSSALSQQIRMDLVTDALVETVSGTEATLIPVNAQTTVCSLADWLAKRGATTRIGPTLESLTKDRAEPNLAPGDENKIAIIGFSGRFPEADNLDEFWDLLIRGLDVHKPVPEERFARDHYDPTGQRKNTSQVQYGCWLKSAGYFDTQFFHMSPKEAMQTDPAQRLALLTAYEALEMAGVVPDRTPSTQRNRVGVYYGTTSNDWGEVNSSQDVDTYYIPGANRAFIPGRVNYFFKFTGPSIAVDTACSSSLAAINLAITSLKNRDCDTAIAGGTNVMTNPDNFAGLDRGHFLSRTGNCKAFDDGADGYCRADGIGTLILKRLPDAIADSDPIFGVILGAHTNHSAESVSITRPLADAQEYLFKKLLNETGIHPHDVSYVEMHGTGTQAGDAVEMRSVLNSFAFDHSRPRDKSLYLGSVKANVGHAESASGVLAIIKVLLMMQKNTIPPHCGIKTKINQGFPKDLDHRGVRIALKDSVDWSRPEGGKRRVLVNNFSAAGGNTSLLLEDGPAVHPARQHQDGDARTEHVVAVSARSTKALEENLKALEAYIANSWAPEGELLSQLSYTTTARRVHHSRRVAFVTNGLDDLRKSLLKAATDAGQVKGIPAVSPKVGFLFTGQGAQETAMAIGYYKSFSSFRSDIHQLDSIATLQGLPSVLPLIHGTTPVEDLSAVVVQLGTCIIQISLARFWISLGITPQYVIGHSLGEYAALQIAGVLSVNDAIFLCGHRAALLDKKCTAYTHGMVAVKAAADDLRQHISSDLKVEIACVNGAEDTVLSGPNADIESLCGKLTQAGYKLHKLEIPFAFHSSQVDPILDDLEELASQVGFHEPKLPIVSPLLRTLLTGDTLGPQYIRRHCRETVDFLGAIKMAESQGIMDRSGMCIEIGAHPILTRMVKSIIGQDFRCLASLRRKEDHFKTLADSLCALHLAGFSVNWDEYHRDFASSRNVLQLPKYSWQLANYWMQYKYSWCLTKGDAPVENGPVGAVVQARALRLSDSVHNVIEQVHGDKRSSITVESDMHDPSLLAIAQNHRVNGLTMAPSTLFADIAFTLAKHLIQNHGLDTHTNLPSINNMAVEKALIVGETGPQLFRASLDMDWTTMRGSVRIFSVGANGKQTTLHAVCDVAVENPSSHRESWQSNAYLIQRGIKQLVQGASDGSAHMMRRGLLYKIFSNSVQYGSAFQGIEQVWFDSEGLEGTGKVFMPSGKDTFALNPYCCDSLGHITGFIMNCSDSLDLDDHVYINHGWRTLRLVEPYQCDVQYQTYVKMQAVGSDDSTYSGDVHVLRDGKIIGICGGVTFKKVARKVLEMLLPKPSGAKAKHGVVKHVAPEPVKHVVLTPPSTTSHSVGTTSPPEPTESPVGSASGLIQKALEIIADEIGVDISQLTDTTLLADLGVDSLMSLTILGNFREELDLDIPAAQFYEFSTVQDLKSFLGANDQDFSSSNSEAESSASSAASTSPSDHGDDVVEEVKPVVAEIPRSTSTILQGTKHCSQTLFLFPDGAGSATSYVTLPSISSDMRVIGLNSPYLTKPHEFNCALQDITGSYLNEVRRRQPQGPYHLAGWSAGGVSAFDAARQLVSEGEVVESLILIDSPNPVGLGKLPKRMYDFLEKSGIFGAFEMGEEAQAPPDWLFQHFCVFIEALDRYVPEPFEHGMAPKTTIIWAADGVCKNPDDPRPEAQPDDPRGMNWLLNNREDFGPNGWDEFIGAGNISTMAIENANHFTMMREPIASALCAKIRETMGVN

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1629-1654Polar residues
Compositional bias1733-1753Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
HF679027
EMBL· GenBank· DDBJ
CCT67991.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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