FUM17_GIBM7
ID FUM17_GIBM7 Reviewed; 388 AA.
AC W7LKY5; Q8J2Q3;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=Sphingosine N-acyltransferase-like protein FUM17 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000305};
DE AltName: Full=Fumonisin biosynthesis cluster protein 17 {ECO:0000303|PubMed:12620260};
GN Name=FUM17 {ECO:0000303|PubMed:12620260}; ORFNames=FVEG_00327;
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], DISRUPTION PHENOTYPE, 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.
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: Sphingosine N-acyltransferase-like protein; part of the gene
CC cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2
CC (FB2), B3 (FB3), and B4 (FB4), which are carcinogenic mycotoxins
CC (PubMed:12620260). On the basis of the chemical structures of
CC fumonisins and precursor feeding studies, fumonisin biosynthesis is
CC predicted to include at least five groups of biochemical reactions:
CC synthesis of a linear polyketide with a single terminal carbonyl
CC function and methyl groups at C-10 and C-14; condensation of the
CC polyketide with alanine; reduction of the polyketide carbonyl to a
CC hydroxyl; hydroxylation of 2-4 polyketide carbons; and esterification
CC of six-carbon tricarboxylic acids to two of the hydroxyls
CC (PubMed:12620260). The biosynthesis starts with the polyketide synthase
CC FUM1-catalyzed carbon chain assembly from one molecule of acetyl CoA,
CC eight molecules of malonyl CoA, and two molecules of methionine
CC (PubMed:10413619). The C-18 polyketide chain is released from the
CC enzyme by a nucleophilic attack of a carbanion, which is derived from
CC R-carbon of alanine by decarboxylation, on the carbonyl carbon of
CC polyketide acyl chain (PubMed:15137825, PubMed:12720383). This step is
CC catalyzed by a pyridoxal 5'-phosphate-dependent aminoacyl transferase
CC FUM8 (PubMed:15137825, PubMed:12720383). The resultant 3-keto
CC 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). FUM17 is not required for production of fumonosins
CC but may have an indirect role such as self-protection
CC (PubMed:12620260). {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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Does not affect the production of fumonisins B1,
CC B2 and B3 (PubMed:12620260). {ECO:0000269|PubMed:12620260}.
CC -!- SIMILARITY: Belongs to the sphingosine N-acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AF155773; AAN74820.1; -; Genomic_DNA.
DR EMBL; DS022242; EWG36210.1; -; Genomic_DNA.
DR RefSeq; XP_018742401.1; XM_018886765.1.
DR AlphaFoldDB; W7LKY5; -.
DR STRING; 117187.FVEG_00327T0; -.
DR EnsemblFungi; FVEG_00327T0; FVEG_00327T0; FVEG_00327.
DR GeneID; 30058704; -.
DR KEGG; fvr:FVEG_00327; -.
DR VEuPathDB; FungiDB:FVEG_00327; -.
DR eggNOG; KOG1607; Eukaryota.
DR HOGENOM; CLU_028277_4_0_1; -.
DR OMA; QMYTACY; -.
DR OrthoDB; 831082at2759; -.
DR Proteomes; UP000009096; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0050291; F:sphingosine N-acyltransferase activity; IEA:InterPro.
DR GO; GO:0046513; P:ceramide biosynthetic process; IEA:InterPro.
DR InterPro; IPR016439; Lag1/Lac1-like.
DR InterPro; IPR006634; TLC-dom.
DR InterPro; IPR013599; TRAM1.
DR PANTHER; PTHR12560; PTHR12560; 1.
DR Pfam; PF08390; TRAM1; 1.
DR Pfam; PF03798; TRAM_LAG1_CLN8; 1.
DR PIRSF; PIRSF005225; LAG1_LAC1; 1.
DR SMART; SM00724; TLC; 1.
DR PROSITE; PS50922; TLC; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..388
FT /note="Sphingosine N-acyltransferase-like protein FUM17"
FT /id="PRO_0000441151"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 151..368
FT /note="TLC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00205"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 388 AA; 45498 MW; ED35E6511A6FB333 CRC64;
MFKATTSARH RPGQGNSLST LMARYNNQGL QRYSLKDKEH KIRRRKRSWG FQHSVILKNS
WALPLLLTIV LPVIYAIHPV ESKFFGHFIL LSYRHGSVTD GMAFPVAQYK KGLWDLAFVA
FYANALFLAR KFIMKRLLRP LALKNNVSTM GKQQRFMEQM YTACYFAVMG PFGLYVMKTT
PGLWIFQTHG MYDSYPHRSL GPAIKFYYLL QAAYWVQQSV VLVLRLEKPR KDHMELTVHH
IITITLIALS YRFHFTHIGI SMYITHDISD LFLATSKSLN YLSHRLQTPA FCLCVIAWIY
LRHYTNWRIL YSVLTEFRTV GPFELDWEAE QYKCQLSQFI TFGLLATLQT LNIIWLYCLL
RNAYRLLFLR IAKDDRSDTD KSEIEHGD
