FUM16_GIBM7
ID FUM16_GIBM7 Reviewed; 676 AA.
AC W7L9F0; Q8J2Q4;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Acyl-CoA synthetase FUM16 {ECO:0000303|PubMed:12620260};
DE EC=6.2.1.- {ECO:0000305|PubMed:12620260};
DE AltName: Full=Fumonisin biosynthesis cluster protein 16 {ECO:0000303|PubMed:12620260};
DE AltName: Full=Long-chain-fatty-acid--CoA ligase FUM16 {ECO:0000305};
GN Name=FUM16 {ECO:0000303|PubMed:12620260}; ORFNames=FVEG_00326;
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC STRAIN=M3125 / FGSC 7600;
RX PubMed=12620260; DOI=10.1016/s1087-1845(02)00525-x;
RA Proctor R.H., Brown D.W., Plattner R.D., Desjardins A.E.;
RT "Co-expression of 15 contiguous genes delineates a fumonisin biosynthetic
RT gene cluster in Gibberella moniliformis.";
RL Fungal Genet. Biol. 38:237-249(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3125 / FGSC 7600;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP FUNCTION.
RC STRAIN=M3125 / FGSC 7600;
RX PubMed=10413619; DOI=10.1006/fgbi.1999.1141;
RA Proctor R.H., Desjardins A.E., Plattner R.D., Hohn T.M.;
RT "A polyketide synthase gene required for biosynthesis of fumonisin
RT mycotoxins in Gibberella fujikuroi mating population A.";
RL Fungal Genet. Biol. 27:100-112(1999).
RN [4]
RP FUNCTION.
RX PubMed=14602658; DOI=10.1128/aem.69.11.6935-6937.2003;
RA Butchko R.A., Plattner R.D., Proctor R.H.;
RT "FUM9 is required for C-5 hydroxylation of fumonisins and complements the
RT meitotically defined Fum3 locus in Gibberella moniliformis.";
RL Appl. Environ. Microbiol. 69:6935-6937(2003).
RN [5]
RP FUNCTION.
RX PubMed=12720383; DOI=10.1021/jf0262007;
RA Butchko R.A., Plattner R.D., Proctor R.H.;
RT "FUM13 encodes a short chain dehydrogenase/reductase required for C-3
RT carbonyl reduction during fumonisin biosynthesis in Gibberella
RT moniliformis.";
RL J. Agric. Food Chem. 51:3000-3006(2003).
RN [6]
RP FUNCTION.
RX PubMed=15066782; DOI=10.1128/aem.70.4.1931-1934.2004;
RA Ding Y., Bojja R.S., Du L.;
RT "Fum3p, a 2-ketoglutarate-dependent dioxygenase required for C-5
RT hydroxylation of fumonisins in Fusarium verticillioides.";
RL Appl. Environ. Microbiol. 70:1931-1934(2004).
RN [7]
RP FUNCTION.
RX PubMed=15137825; DOI=10.1021/jf035429z;
RA Bojja R.S., Cerny R.L., Proctor R.H., Du L.;
RT "Determining the biosynthetic sequence in the early steps of the fumonisin
RT pathway by use of three gene-disruption mutants of Fusarium
RT verticillioides.";
RL J. Agric. Food Chem. 52:2855-2860(2004).
RN [8]
RP FUNCTION.
RX PubMed=15969533; DOI=10.1021/jf050062e;
RA Yi H., Bojja R.S., Fu J., Du L.;
RT "Direct evidence for the function of FUM13 in 3-ketoreduction of mycotoxin
RT fumonisins in Fusarium verticillioides.";
RL J. Agric. Food Chem. 53:5456-5460(2005).
RN [9]
RP FUNCTION.
RX PubMed=16489749; DOI=10.1021/bi052085s;
RA Zaleta-Rivera K., Xu C., Yu F., Butchko R.A., Proctor R.H.,
RA Hidalgo-Lara M.E., Raza A., Dussault P.H., Du L.;
RT "A bidomain nonribosomal peptide synthetase encoded by FUM14 catalyzes the
RT formation of tricarballylic esters in the biosynthesis of fumonisins.";
RL Biochemistry 45:2561-2569(2006).
RN [10]
RP FUNCTION.
RX PubMed=16536629; DOI=10.1021/jf0527706;
RA Proctor R.H., Plattner R.D., Desjardins A.E., Busman M., Butchko R.A.;
RT "Fumonisin production in the maize pathogen Fusarium verticillioides:
RT genetic basis of naturally occurring chemical variation.";
RL J. Agric. Food Chem. 54:2424-2430(2006).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17147424; DOI=10.1021/jf0617869;
RA Butchko R.A., Plattner R.D., Proctor R.H.;
RT "Deletion analysis of FUM genes involved in tricarballylic ester formation
RT during fumonisin biosynthesis.";
RL J. Agric. Food Chem. 54:9398-9404(2006).
CC -!- FUNCTION: Acyl-CoA synthetase; part of the gene cluster that mediates
CC the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), and B4
CC (FB4), which are carcinogenic mycotoxins (PubMed:12620260). On the
CC basis of the chemical structures of fumonisins and precursor feeding
CC studies, fumonisin biosynthesis is predicted to include at least five
CC groups of biochemical reactions: synthesis of a linear polyketide with
CC a single terminal carbonyl function and methyl groups at C-10 and C-14;
CC condensation of the polyketide with alanine; reduction of the
CC polyketide carbonyl to a hydroxyl; hydroxylation of 2-4 polyketide
CC carbons; and esterification of six-carbon tricarboxylic acids to two of
CC the hydroxyls (PubMed:12620260). The biosynthesis starts with the
CC polyketide synthase FUM1-catalyzed carbon chain assembly from one
CC molecule of acetyl CoA, eight molecules of malonyl CoA, and two
CC molecules of methionine (PubMed:10413619). The C-18 polyketide chain is
CC released from the enzyme by a nucleophilic attack of a carbanion, which
CC is derived from R-carbon of alanine by decarboxylation, on the carbonyl
CC carbon of polyketide acyl chain (PubMed:15137825, PubMed:12720383).
CC This step is catalyzed by a pyridoxal 5'-phosphate-dependent aminoacyl
CC transferase FUM8 (PubMed:15137825, PubMed:12720383). The resultant 3-
CC keto intermediate 2-amino-3-oxo-12,16-dimethylicosane is then
CC stereospecifically reduced to the 3-hydroxyl product 2-amino-3-hydroxy-
CC 12,16-dimethylicosane by reductase FUM13 (PubMed:12720383,
CC PubMed:15137825). Subsequent oxidations at C-5, C-10, C-14 and C-15
CC followed by tricarballylic esterification of the hydroxyl groups on C-
CC 14 and C-15 furnish the biosynthesis of fumonisins (PubMed:15066782,
CC PubMed:15137825, PubMed:16489749). The C-10 hydroxylation is performed
CC by the cytochrome P450 monooxygenase FUM2 and occurs early in the
CC biosynthesis (PubMed:16536629). The C-5 hydroxylation is performed by
CC the dioxygenase FUM3 and occurs late in the biosynthesis
CC (PubMed:20237561, PubMed:15066782, PubMed:15137825, PubMed:16536629).
CC Cytochrome P450 monooxygenases FUM6 and FUM15 may be responsible for
CC the two remaining hydroxylations at positions C-14 and C-15
CC (PubMed:12620260). The FUM11 tricarboxylate transporter makes a
CC tricarboxylic acid precursor available for fumonisin biosynthesis via
CC its export from the mitochondria (PubMed:12620260). If the precursor is
CC citrate, the FUM7 dehydrogenase could remove the C-3 hydroxyl of
CC citrate to form tricarballylic acid either before or after the CoA
CC activation by the FUM10 acyl-CoA synthetase and FUM14 catalyzed
CC esterification of CoA-activated tricarballylic acid to the C-14 and C-
CC 15 hydroxyls of the fumonisin backbone (PubMed:16489749,
CC PubMed:17147424). Alternatively, if the precursor is cis-aconitate,
CC FUM7 may function to reduce the double bond (PubMed:17147424). In this
CC alternate proposal, feeding studies with tetradehydro-fumonisin B1
CC suggests that FUM7 cannot function on the tricarballylic ester and must
CC therefore act before the FUM14-mediated esterification
CC (PubMed:17147424). {ECO:0000269|PubMed:10413619,
CC ECO:0000269|PubMed:12620260, ECO:0000269|PubMed:12720383,
CC ECO:0000269|PubMed:14602658, ECO:0000269|PubMed:15066782,
CC ECO:0000269|PubMed:15137825, ECO:0000269|PubMed:15969533,
CC ECO:0000269|PubMed:16489749, ECO:0000269|PubMed:16536629,
CC ECO:0000269|PubMed:17147424}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:12620260}.
CC -!- DISRUPTION PHENOTYPE: Does not affect fumonisin production
CC (PubMed:17147424). {ECO:0000269|PubMed:17147424}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AF155773; AAN74819.2; -; Genomic_DNA.
DR EMBL; DS022242; EWG36208.1; -; Genomic_DNA.
DR RefSeq; XP_018742399.1; XM_018886763.1.
DR AlphaFoldDB; W7L9F0; -.
DR SMR; W7L9F0; -.
DR STRING; 117187.FVEG_00326T0; -.
DR GeneID; 30058703; -.
DR KEGG; fvr:FVEG_00326; -.
DR VEuPathDB; FungiDB:FVEG_00326; -.
DR eggNOG; KOG1180; Eukaryota.
DR OrthoDB; 293865at2759; -.
DR Proteomes; UP000009096; Chromosome 1.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..676
FT /note="Acyl-CoA synthetase FUM16"
FT /id="PRO_0000441149"
FT REGION 552..655
FT /note="AMP-binding"
FT /evidence="ECO:0000255"
FT BINDING 245..256
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255"
SQ SEQUENCE 676 AA; 74927 MW; A509BC95F7FB51B7 CRC64;
MYHTVPYTIE SPGYLKVAGE SLPRRHPRAK HGLLRYPSAG VLTVFDIVRR SAKLYPDNKA
VGSRRLIKMH REFKIIQDKE KEWIYYELGP YNYLSYSQYE LLAIQIGSGL RKLGLSSSNK
VYLFGTTSAN WISMSHGCAS QGIPIVTGYD TLSATDIQHS LSQTHAEVIY LDPHLLGTAS
IALENSQVKT VIINTGSIFS GGYDIDQFRN EHPQFNVITY EELIQLGRHN LKEPIPVKSS
DLFCIMYTSG STGLPNGCCI THENFLAGIT GLLGGIDDFV SDQERVLAYL PLAHIFEMAL
ENLVMYIGGT LGYGNPKTLT DASLRECNGD MVEFKPTIMV GVPQIWETIR KAVLSKLNCS
GFVAKTVFWT AMSFKSFAVR YSLPGKGVFD DLVFGRVRQM TGGRLRYILN GSSGIADSTK
EFLSLIVAEM LTGYGLTETC ANGALSSPFE QTTSAIGSTS PAIDVKLVSI PELGYFTDAD
AGPCQGEILV RGPAVFKGYF NNPQGTEKAF APGGWFKTGD IGEFDDRGHL KIIDRIKSLV
KMQGGEYIAL EKLESIYRTS QAILQVMVHA DFEYTRPIVI IMPNTKFLQD KSRELGFSDD
DSTLSSERMS AYVLDDLQDI ARRSGLSKIE TVTGVVITDI EWTPQSGLVT PTMKLNRRFI
LNYFRDEVEK CMQSIG
