FUM11_GIBM7
ID FUM11_GIBM7 Reviewed; 306 AA.
AC Q8J2Q9; W7LUF8;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Tricarboxylate transporter FUM11 {ECO:0000303|PubMed:12620260};
DE AltName: Full=Fumonisin biosynthesis cluster protein 11 {ECO:0000303|PubMed:12620260};
GN Name=FUM11 {ECO:0000303|PubMed:12620260}; ORFNames=FVEG_00322;
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, DISRUPTION PHENOTYPE, AND PATHWAY.
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: Tricarboxylate transporter; part of the gene cluster that
CC mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3),
CC and B4 (FB4), which are carcinogenic mycotoxins (PubMed:12620260,
CC PubMed:17147424). On the basis of the chemical structures of fumonisins
CC and precursor feeding studies, fumonisin biosynthesis is predicted to
CC include at least five groups of biochemical reactions: synthesis of a
CC linear polyketide with a single terminal carbonyl function and methyl
CC groups at C-10 and C-14; condensation of the polyketide with alanine;
CC reduction of the polyketide carbonyl to a hydroxyl; hydroxylation of 2-
CC 4 polyketide carbons; and esterification of six-carbon tricarboxylic
CC acids to two of the hydroxyls (PubMed:12620260). The biosynthesis
CC starts with the polyketide synthase FUM1-catalyzed carbon chain
CC assembly from one molecule of acetyl CoA, eight molecules of malonyl
CC CoA, and two molecules of methionine (PubMed:10413619). The C-18
CC polyketide chain is released from the enzyme by a nucleophilic attack
CC of a carbanion, which is derived from R-carbon of alanine by
CC decarboxylation, on the carbonyl carbon of polyketide acyl chain
CC (PubMed:15137825, PubMed:12720383). This step is catalyzed by a
CC pyridoxal 5'-phosphate-dependent aminoacyl transferase FUM8
CC (PubMed:15137825, PubMed:12720383). The resultant 3-keto intermediate
CC 2-amino-3-oxo-12,16-dimethylicosane is then stereospecifically reduced
CC to the 3-hydroxyl product 2-amino-3-hydroxy-12,16-dimethylicosane by
CC reductase FUM13 (PubMed:12720383, PubMed:15137825). Subsequent
CC oxidations at C-5, C-10, C-14 and C-15 followed by tricarballylic
CC esterification of the hydroxyl groups on C-14 and C-15 furnish the
CC biosynthesis of fumonisins (PubMed:15066782, PubMed:15137825,
CC PubMed:16489749). The C-10 hydroxylation is performed by the cytochrome
CC P450 monooxygenase FUM2 and occurs early in the biosynthesis
CC (PubMed:16536629). The C-5 hydroxylation is performed by the
CC dioxygenase FUM3 and occurs late in the biosynthesis (PubMed:20237561,
CC PubMed:15066782, PubMed:15137825, PubMed:16536629). Cytochrome P450
CC monooxygenases FUM6 and FUM15 may be responsible for the two remaining
CC hydroxylations at positions C-14 and C-15 (PubMed:12620260). The FUM11
CC tricarboxylate transporter makes a tricarboxylic acid precursor
CC available for fumonisin biosynthesis via its export from the
CC mitochondria (PubMed:12620260). If the precursor is citrate, the FUM7
CC dehydrogenase could remove the C-3 hydroxyl of citrate to form
CC tricarballylic acid either before or after the CoA activation by the
CC FUM10 acyl-CoA synthetase and FUM14 catalyzed esterification of CoA-
CC activated tricarballylic acid to the C-14 and C-15 hydroxyls of the
CC fumonisin backbone (PubMed:16489749, PubMed:17147424). Alternatively,
CC if the precursor is cis-aconitate, FUM7 may function to reduce the
CC double bond (PubMed:17147424). In this alternate proposal, feeding
CC studies with tetradehydro-fumonisin B1 suggests that FUM7 cannot
CC function on the tricarballylic ester and must therefore act before the
CC FUM14-mediated esterification (PubMed:17147424).
CC {ECO:0000269|PubMed:10413619, ECO:0000269|PubMed:12620260,
CC ECO:0000269|PubMed:12720383, ECO:0000269|PubMed:14602658,
CC ECO:0000269|PubMed:15066782, ECO:0000269|PubMed:15137825,
CC ECO:0000269|PubMed:15969533, ECO:0000269|PubMed:16489749,
CC ECO:0000269|PubMed:16536629, ECO:0000269|PubMed:17147424}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:12620260,
CC ECO:0000269|PubMed:17147424}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Produces fumonisins that lack one of the
CC tricarballylic ester functions (PubMed:17147424).
CC {ECO:0000269|PubMed:17147424}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EWG36202.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF155773; AAN74814.2; -; Genomic_DNA.
DR EMBL; DS022242; EWG36202.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_018742393.1; XM_018886759.1.
DR AlphaFoldDB; Q8J2Q9; -.
DR SMR; Q8J2Q9; -.
DR STRING; 117187.FVEG_00322T0; -.
DR GeneID; 30058699; -.
DR KEGG; fvr:FVEG_00322; -.
DR eggNOG; KOG0756; Eukaryota.
DR OMA; FICARGI; -.
DR OrthoDB; 1523221at2759; -.
DR Proteomes; UP000009096; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1900541; P:fumonisin biosynthetic process; IMP:GO_Central.
DR Gene3D; 1.50.40.10; -; 2.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR Pfam; PF00153; Mito_carr; 3.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 3: Inferred from homology;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..306
FT /note="Tricarboxylate transporter FUM11"
FT /id="PRO_0000441150"
FT TRANSMEM 24..44
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..189
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..286
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 18..98
FT /note="Solcar 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 109..195
FT /note="Solcar 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT REPEAT 206..292
FT /note="Solcar 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
SQ SEQUENCE 306 AA; 33582 MW; B4C7CD86CE35315C CRC64;
MSLYDKSVTA TRSAHRTSDT LHSLVAGSVA GGLEIAITYP AEFAKTRLQL NQVSGRNKQN
VPWPRFGLQW YSGCIPFLIG NSVKTSIRFV SFDGYQKLLA DDDGNISRFG ILLAGFGAGA
TESLLAVTPS ERIKTIIIED RRLEKPRIRN SFHAMSIIAR DHGLSGFFQG FWPTTARQSA
GSAIRLGSYT FLKQVVQSRT PQGGKIGTVK TFIIGSLAGL ITVYLTQPLD TIKTRMQRLE
ARTRYGNAFI CARGILEQEG FTAFWSGAVA RSLRLVMSGG IVFMVYEKVV EGLDVISPAK
RYEIAA
