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Protein

Acyl-CoA synthetase FUM16

Gene

FUM16

Organism
Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot fungus) (Fusarium verticillioides)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

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:15137825, PubMed:12720383). This step is catalyzed by a pyridoxal 5'-phosphate-dependent aminoacyl transferase FUM8 (PubMed:15137825, PubMed:12720383). 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:20237561, PubMed:15066782, PubMed:15137825, PubMed:16536629). 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).10 Publications

Pathwayi: Mycotoxin biosynthesis

This protein is involved in Mycotoxin biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in Mycotoxin biosynthesis.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigase
LigandATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA synthetase FUM161 Publication (EC:6.2.1.-1 Publication)
Alternative name(s):
Fumonisin biosynthesis cluster protein 161 Publication
Long-chain-fatty-acid--CoA ligase FUM16Curated
Gene namesi
Name:FUM161 Publication
ORF Names:FVEG_00326
OrganismiGibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot fungus) (Fusarium verticillioides)
Taxonomic identifieri334819 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaeFusariumFusarium fujikuroi species complex
Proteomesi
  • UP000009096 Componentsi: Chromosome 1, Unassembled WGS sequence

Pathology & Biotechi

Disruption phenotypei

Does not affect fumonisin production (PubMed:17147424).1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004411491 – 676Acyl-CoA synthetase FUM16Add BLAST676

Structurei

3D structure databases

ProteinModelPortaliW7L9F0
SMRiW7L9F0
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni245 – 256AMP-bindingSequence analysisAdd BLAST12
Regioni552 – 655AMP-bindingSequence analysisAdd BLAST104

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1180 Eukaryota
COG1022 LUCA
KOiK01897

Family and domain databases

InterProiView protein in InterPro
IPR000873 AMP-dep_Synth/Lig
PfamiView protein in Pfam
PF00501 AMP-binding, 1 hit

Sequencei

Sequence statusi: Complete.

W7L9F0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYHTVPYTIE SPGYLKVAGE SLPRRHPRAK HGLLRYPSAG VLTVFDIVRR
60 70 80 90 100
SAKLYPDNKA VGSRRLIKMH REFKIIQDKE KEWIYYELGP YNYLSYSQYE
110 120 130 140 150
LLAIQIGSGL RKLGLSSSNK VYLFGTTSAN WISMSHGCAS QGIPIVTGYD
160 170 180 190 200
TLSATDIQHS LSQTHAEVIY LDPHLLGTAS IALENSQVKT VIINTGSIFS
210 220 230 240 250
GGYDIDQFRN EHPQFNVITY EELIQLGRHN LKEPIPVKSS DLFCIMYTSG
260 270 280 290 300
STGLPNGCCI THENFLAGIT GLLGGIDDFV SDQERVLAYL PLAHIFEMAL
310 320 330 340 350
ENLVMYIGGT LGYGNPKTLT DASLRECNGD MVEFKPTIMV GVPQIWETIR
360 370 380 390 400
KAVLSKLNCS GFVAKTVFWT AMSFKSFAVR YSLPGKGVFD DLVFGRVRQM
410 420 430 440 450
TGGRLRYILN GSSGIADSTK EFLSLIVAEM LTGYGLTETC ANGALSSPFE
460 470 480 490 500
QTTSAIGSTS PAIDVKLVSI PELGYFTDAD AGPCQGEILV RGPAVFKGYF
510 520 530 540 550
NNPQGTEKAF APGGWFKTGD IGEFDDRGHL KIIDRIKSLV KMQGGEYIAL
560 570 580 590 600
EKLESIYRTS QAILQVMVHA DFEYTRPIVI IMPNTKFLQD KSRELGFSDD
610 620 630 640 650
DSTLSSERMS AYVLDDLQDI ARRSGLSKIE TVTGVVITDI EWTPQSGLVT
660 670
PTMKLNRRFI LNYFRDEVEK CMQSIG
Length:676
Mass (Da):74,927
Last modified:April 16, 2014 - v1
Checksum:iA509BC95F7FB51B7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF155773 Genomic DNA Translation: AAN74819.2
DS022242 Genomic DNA Translation: EWG36208.1
RefSeqiXP_018742399.1, XM_018886763.1

Genome annotation databases

GeneIDi30058703
KEGGifvr:FVEG_00326

Similar proteinsi

Entry informationi

Entry nameiFUM16_GIBM7
AccessioniPrimary (citable) accession number: W7L9F0
Secondary accession number(s): Q8J2Q4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 30, 2017
Last sequence update: April 16, 2014
Last modified: November 22, 2017
This is version 17 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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