W7L9F0 · FUM16_GIBM7

Function

function

Acyl-CoA synthetase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), and B4 (FB4), which are carcinogenic mycotoxins (PubMed:12620260).
On the basis of the chemical structures of fumonisins and precursor feeding studies, fumonisin biosynthesis is predicted to include at least five groups of biochemical reactions: synthesis of a linear polyketide with a single terminal carbonyl function and methyl groups at C-10 and C-14; condensation of the polyketide with alanine; reduction of the polyketide carbonyl to a hydroxyl; hydroxylation of 2-4 polyketide carbons; and esterification of six-carbon tricarboxylic acids to two of the hydroxyls (PubMed:12620260).
The biosynthesis starts with the polyketide synthase FUM1-catalyzed carbon chain assembly from one molecule of acetyl CoA, eight molecules of malonyl CoA, and two molecules of methionine (PubMed:10413619).
The C-18 polyketide chain is released from the enzyme by a nucleophilic attack of a carbanion, which is derived from R-carbon of alanine by decarboxylation, on the carbonyl carbon of polyketide acyl chain (PubMed:12720383, PubMed:15137825).
This step is catalyzed by a pyridoxal 5'-phosphate-dependent aminoacyl transferase FUM8 (PubMed:12720383, PubMed:15137825).
The resultant 3-keto intermediate 2-amino-3-oxo-12,16-dimethylicosane is then stereospecifically reduced to the 3-hydroxyl product 2-amino-3-hydroxy-12,16-dimethylicosane by reductase FUM13 (PubMed:12720383, PubMed:15137825).
Subsequent oxidations at C-5, C-10, C-14 and C-15 followed by tricarballylic esterification of the hydroxyl groups on C-14 and C-15 furnish the biosynthesis of fumonisins (PubMed:15066782, PubMed:15137825, PubMed:16489749).
The C-10 hydroxylation is performed by the cytochrome P450 monooxygenase FUM2 and occurs early in the biosynthesis (PubMed:16536629).
The C-5 hydroxylation is performed by the dioxygenase FUM3 and occurs late in the biosynthesis (PubMed:15066782, PubMed:15137825, PubMed:16536629, PubMed:20237561).
Cytochrome P450 monooxygenases FUM6 and FUM15 may be responsible for the two remaining hydroxylations at positions C-14 and C-15 (PubMed:12620260).
The FUM11 tricarboxylate transporter makes a tricarboxylic acid precursor available for fumonisin biosynthesis via its export from the mitochondria (PubMed:12620260).
If the precursor is citrate, the FUM7 dehydrogenase could remove the C-3 hydroxyl of citrate to form tricarballylic acid either before or after the CoA activation by the FUM10 acyl-CoA synthetase and FUM14 catalyzed esterification of CoA-activated tricarballylic acid to the C-14 and C-15 hydroxyls of the fumonisin backbone (PubMed:16489749, PubMed:17147424).
Alternatively, if the precursor is cis-aconitate, FUM7 may function to reduce the double bond (PubMed:17147424).
In this alternate proposal, feeding studies with tetradehydro-fumonisin B1 suggests that FUM7 cannot function on the tricarballylic ester and must therefore act before the FUM14-mediated esterification (PubMed:17147424).

Pathway

Mycotoxin biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site245-256AMP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentendoplasmic reticulum
Cellular Componentlipid droplet
Cellular Componentplasma membrane
Molecular FunctionATP binding
Molecular Functionlong-chain fatty acid-CoA ligase activity
Biological Processlong-chain fatty-acyl-CoA metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Acyl-CoA synthetase FUM16
  • EC number
  • Alternative names
    • Fumonisin biosynthesis cluster protein 16
    • Long-chain-fatty-acid--CoA ligase FUM16

Gene names

    • Name
      FUM16
    • ORF names
      FVEG_00326

Organism names

Accessions

  • Primary accession
    W7L9F0
  • Secondary accessions
    • Q8J2Q4

Proteomes

Organism-specific databases

Phenotypes & Variants

Disruption phenotype

Does not affect fumonisin production (PubMed:17147424).

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004411491-676Acyl-CoA synthetase FUM16

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region552-655AMP-binding

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    676
  • Mass (Da)
    74,927
  • Last updated
    2014-04-16 v1
  • Checksum
    A509BC95F7FB51B7
MYHTVPYTIESPGYLKVAGESLPRRHPRAKHGLLRYPSAGVLTVFDIVRRSAKLYPDNKAVGSRRLIKMHREFKIIQDKEKEWIYYELGPYNYLSYSQYELLAIQIGSGLRKLGLSSSNKVYLFGTTSANWISMSHGCASQGIPIVTGYDTLSATDIQHSLSQTHAEVIYLDPHLLGTASIALENSQVKTVIINTGSIFSGGYDIDQFRNEHPQFNVITYEELIQLGRHNLKEPIPVKSSDLFCIMYTSGSTGLPNGCCITHENFLAGITGLLGGIDDFVSDQERVLAYLPLAHIFEMALENLVMYIGGTLGYGNPKTLTDASLRECNGDMVEFKPTIMVGVPQIWETIRKAVLSKLNCSGFVAKTVFWTAMSFKSFAVRYSLPGKGVFDDLVFGRVRQMTGGRLRYILNGSSGIADSTKEFLSLIVAEMLTGYGLTETCANGALSSPFEQTTSAIGSTSPAIDVKLVSIPELGYFTDADAGPCQGEILVRGPAVFKGYFNNPQGTEKAFAPGGWFKTGDIGEFDDRGHLKIIDRIKSLVKMQGGEYIALEKLESIYRTSQAILQVMVHADFEYTRPIVIIMPNTKFLQDKSRELGFSDDDSTLSSERMSAYVLDDLQDIARRSGLSKIETVTGVVITDIEWTPQSGLVTPTMKLNRRFILNYFRDEVEKCMQSIG

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
W7LL87W7LL87_GIBM7FVEG_00326543

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF155773
EMBL· GenBank· DDBJ
AAN74819.2
EMBL· GenBank· DDBJ
Genomic DNA
CM000578
EMBL· GenBank· DDBJ
EWG36208.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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