FUB1_GIBM7
ID FUB1_GIBM7 Reviewed; 2409 AA.
AC W7MT31;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Reducing polyketide synthase FUB1 {ECO:0000303|PubMed:22652150};
DE EC=2.3.1.- {ECO:0000305|PubMed:22652150};
DE AltName: Full=Fusaric acid biosynthesis protein 1 {ECO:0000303|PubMed:22652150};
GN Name=FUB1 {ECO:0000303|PubMed:22652150}; ORFNames=FVEG_12523;
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 [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 [2]
RP BIOTECHNOLOGY.
RX PubMed=16868776; DOI=10.1007/s00425-006-0345-6;
RA Samadi L., Shahsavan Behboodi B.;
RT "Fusaric acid induces apoptosis in saffron root-tip cells: roles of
RT caspase-like activity, cytochrome c, and H2O2.";
RL Planta 225:223-234(2006).
RN [3]
RP BIOTECHNOLOGY.
RX PubMed=17927749; DOI=10.1111/j.1365-2672.2007.03581.x;
RA Son S.W., Kim H.Y., Choi G.J., Lim H.K., Jang K.S., Lee S.O., Lee S.,
RA Sung N.D., Kim J.C.;
RT "Bikaverin and fusaric acid from Fusarium oxysporum show antioomycete
RT activity against Phytophthora infestans.";
RL J. Appl. Microbiol. 104:692-698(2008).
RN [4]
RP BIOTECHNOLOGY.
RX PubMed=21811925; DOI=10.1007/s12272-011-0716-9;
RA Pan J.H., Chen Y., Huang Y.H., Tao Y.W., Wang J., Li Y., Peng Y., Dong T.,
RA Lai X.M., Lin Y.C.;
RT "Antimycobacterial activity of fusaric acid from a mangrove endophyte and
RT its metal complexes.";
RL Arch. Pharm. Res. 34:1177-1181(2011).
RN [5]
RP BIOTECHNOLOGY.
RX PubMed=20955724; DOI=10.1016/j.toxicon.2010.10.006;
RA Stipanovic R.D., Puckhaber L.S., Liu J., Bell A.A.;
RT "Phytotoxicity of fusaric acid and analogs to cotton.";
RL Toxicon 57:176-178(2011).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RX PubMed=22652150; DOI=10.1016/j.fgb.2012.05.010;
RA Brown D.W., Butchko R.A., Busman M., Proctor R.H.;
RT "Identification of gene clusters associated with fusaric acid, fusarin, and
RT perithecial pigment production in Fusarium verticillioides.";
RL Fungal Genet. Biol. 49:521-532(2012).
RN [7]
RP INDUCTION.
RX PubMed=22713715; DOI=10.1016/j.fgb.2012.06.003;
RA Butchko R.A., Brown D.W., Busman M., Tudzynski B., Wiemann P.;
RT "Lae1 regulates expression of multiple secondary metabolite gene clusters
RT in Fusarium verticillioides.";
RL Fungal Genet. Biol. 49:602-612(2012).
RN [8]
RP BIOTECHNOLOGY.
RX PubMed=22864988; DOI=10.1055/s-0032-1315146;
RA Boonman N., Prachya S., Boonmee A., Kittakoop P., Wiyakrutta S.,
RA Sriubolmas N., Warit S., Dharmkrong-At Chusattayanond A.;
RT "In vitro acanthamoebicidal activity of fusaric acid and dehydrofusaric
RT acid from an endophytic fungus Fusarium sp. Tlau3.";
RL Planta Med. 78:1562-1567(2012).
RN [9]
RP BIOTECHNOLOGY.
RX PubMed=23838885; DOI=10.1007/s00425-013-1928-7;
RA Jiao J., Zhou B., Zhu X., Gao Z., Liang Y.;
RT "Fusaric acid induction of programmed cell death modulated through nitric
RT oxide signalling in tobacco suspension cells.";
RL Planta 238:727-737(2013).
RN [10]
RP BIOTECHNOLOGY.
RX PubMed=23922960; DOI=10.1371/journal.pone.0070226;
RA Li C., Zuo C., Deng G., Kuang R., Yang Q., Hu C., Sheng O., Zhang S.,
RA Ma L., Wei Y., Yang J., Liu S., Biswas M.K., Viljoen A., Yi G.;
RT "Contamination of bananas with beauvericin and fusaric acid produced by
RT Fusarium oxysporum f. sp. cubense.";
RL PLoS ONE 8:E70226-E70226(2013).
RN [11]
RP FUNCTION, AND INDUCTION.
RX PubMed=25372119; DOI=10.1094/mpmi-09-14-0264-r;
RA Brown D.W., Lee S.H., Kim L.H., Ryu J.G., Lee S., Seo Y., Kim Y.H.,
RA Busman M., Yun S.H., Proctor R.H., Lee T.;
RT "Identification of a 12-gene fusaric acid biosynthetic gene cluster in
RT Fusarium species through comparative and functional genomics.";
RL Mol. Plant Microbe Interact. 28:319-332(2015).
CC -!- FUNCTION: Reducing polyketide synthase; part of the gene cluster that
CC mediates the biosynthesis of fusaric acid, a mycotoxin with low to
CC moderate toxicity to animals and humans, but with high phytotoxic
CC properties (PubMed:22652150, PubMed:25372119). L-aspartate is suggested
CC as fusaric acid amino acid precursor that is activated and further
CC processed to O-acetyl-L-homoserine by cluster enzymes aspartate kinase
CC FUB3 and homoserine O-acetyltransferase FUB5, as well as enzymes of the
CC primary metabolism (By similarity). The polyketide synthase (PKS) FUB1
CC generates the triketide trans-2-hexenal which is presumptively released
CC by the hydrolase FUB4 and linked to the NRPS-bound amino acid precursor
CC by NAD(P)-dependent dehydrogenase FUB6 (By similarity). FUB1, FUB4, and
CC the non-canonical NRPS Fub8 may form an enzyme complex (By similarity).
CC Further processing of the NRPS-bound intermediate might be carried out
CC by FUB6 and the sulfhydrylase FUB7, enabling a spontaneous
CC electrocyclization to close the carbon backbone of fusaric acid (By
CC similarity). Dihydrofusaric acid is likely to be released via reduction
CC by the thioester reductase (TR) domain of FUB8 whereupon the final
CC oxidation to fusaric acid may (also) be performed by the FMN-dependent
CC dehydrogenase FUB9 (By similarity). {ECO:0000250|UniProtKB:S0DRI1,
CC ECO:0000269|PubMed:22652150, ECO:0000269|PubMed:25372119}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:22652150,
CC ECO:0000269|PubMed:25372119}.
CC -!- INDUCTION: Expression is positively regulated by the fusaric acid
CC cluster specific transcription factor FUB10 (PubMed:25372119).
CC Expression is also positively regulated by the secondary metabolism
CC regulator LAE1 (PubMed:22713715). {ECO:0000269|PubMed:22713715,
CC ECO:0000269|PubMed:25372119}.
CC -!- DOMAIN: Multidomain protein; including a starter unit:ACP transacylase
CC (SAT) that selects the starter unit; a ketosynthase (KS) that catalyzes
CC repeated decarboxylative condensation to elongate the polyketide
CC backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and
CC transfers the extender unit malonyl-CoA; a product template (PT) domain
CC that controls the immediate cyclization regioselectivity of the
CC reactive polyketide backbone; and an acyl-carrier protein (ACP) that
CC serves as the tether of the growing and completed polyketide via its
CC phosphopantetheinyl arm. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of fusaric acid
CC (PubMed:22652150). {ECO:0000269|PubMed:22652150}.
CC -!- BIOTECHNOLOGY: Fusaric acid is phytotoxic to plants such as cotton and
CC banana (PubMed:20955724, PubMed:23922960). It has been shown to induce
CC programmed cell death in plants (PubMed:16868776, PubMed:23838885). In
CC addition to a mild toxicity to animals, fusaric acid exhibits
CC acanthamoebicidal, antioomycete, and antimycobacterial activities
CC (PubMed:17927749, PubMed:22864988, PubMed:21811925).
CC {ECO:0000269|PubMed:16868776, ECO:0000269|PubMed:17927749,
CC ECO:0000269|PubMed:20955724, ECO:0000269|PubMed:21811925,
CC ECO:0000269|PubMed:22864988, ECO:0000269|PubMed:23838885,
CC ECO:0000269|PubMed:23922960}.
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DR EMBL; DS022261; EWG54266.1; -; Genomic_DNA.
DR RefSeq; XP_018760457.1; XM_018901864.1.
DR AlphaFoldDB; W7MT31; -.
DR SMR; W7MT31; -.
DR STRING; 117187.FVEG_12523T0; -.
DR GeneID; 30069957; -.
DR KEGG; fvr:FVEG_12523; -.
DR VEuPathDB; FungiDB:FVEG_12523; -.
DR eggNOG; KOG1202; Eukaryota.
DR OrthoDB; 19161at2759; -.
DR BioCyc; MetaCyc:MON-19345; -.
DR PHI-base; PHI:3387; -.
DR Proteomes; UP000009096; Chromosome 3.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 2.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Multifunctional enzyme; NADP; Oxidoreductase;
KW Phosphopantetheine; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..2409
FT /note="Reducing polyketide synthase FUB1"
FT /id="PRO_0000437308"
FT DOMAIN 2328..2405
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..482
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 608..929
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 995..1302
FT /note="Dehydrogenase (DH) domain"
FT /evidence="ECO:0000255"
FT REGION 1713..2025
FT /note="Enoyl reductase (ER) domain"
FT /evidence="ECO:0000255"
FT REGION 2049..2225
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 230
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 699
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 1026
FT /note="For beta-hydroxyacyl dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2365
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2409 AA; 260134 MW; 2183CC2D58BCF720 CRC64;
MTLSNGSNGA NGTSNGHGAH PSANGFHNAA NGGANNGTPN GGAEYNASLP QVDGDISSAI
AVIGVSGRFP GDATSPRHLW DLLKEGRNAL SDVPESRFNI DGFYHPDGGR AGTLNTKQGY
FLKSDVDKFD AGFFSITPEE ARGMDPTQRI LLELAYEGLE NAGLKIDEVA NQHMSCYIGA
CQHDYWDLQA YDMDSAPKYT ATGTGPALLS NRISWFFNLK GPSVTIDTAC SSTLTALHLA
GQSIRNGESD SALVGGLGLH LLPNFGVFMS SMSFLSADNK CHSFDASANG YARAEGGGFV
VLKRLDKALA DGDTIRAVLR STGSNQDGRT LGITQPSASR QEELIRATYA SAGLTFDKTN
FFEAHGTGTK VGDPIECSVI GNVFGKTRER PVYVGSVKSN IGHLEGASGL AGLVKTIYSL
ESGVISPTYG LENVNPKIKL DEWKINLPTE KIKWPAGLRR ASINSFGYGG ANAHAVLDDA
YHFLKTHNLE GHHNTKAEDV PATGLIGNGS QDIIEKTDKK PRLFLISSHE ESGIARLSQT
LQAYLADPAA RDLPEDQFLH RLAYTLSEKR SSLPWKTYAA ASTIEELQQA LDGAPTKAAR
VPRSQALTFI FTGQGAQWFA MGRELQKYPI FRQSLHACSQ YLKDFGSTWD LVEELNRDAK
ESIIDLPYVS QPSCTALQLS IIDLLASWGI HPQVTVGHSS GEIAAAYAKG AFDKEAAMRI
AYFRGHLTGN ITKTGSMAAV GLGPERVSEY LSRVTAGKIV VACINSPASV TLSGDVEGID
EVLTFLQADD IFARKLRVTT AYHSHHMQQI SEEYLNSLSG KWELKPGNPK VRMFSSVSAK
PIDGTELGPA YWVANLVSPV NFSGAVTAAA NAGALGKRKA SGKKGSADAM VEIGPHAALQ
GPLKQILDSI GDKGASPKYF SAIKRKQDAI QTTLEVVGEL LVLGHQVNVP LVNAYTETTS
ALVDLPPYAW NTTNSYWHES AAVTAYKQRK HPRLELLGVR DPRSTKAEPA WHNYLRISEQ
PWIEHHQFQN TNIYPMAGMI VMAIEGLRQV ETRTDVEGYT IRDVNIGSAL VVPLDQTIET
RLQLTPWRSG PNVSWSHWTE FTVSSRNESG SWTTNCTGLV STSYKRETNS TFLDEEAAAN
ALLSQEYKAI SNSDLPSVDP TVFYTKLDES GFSLGPAFRG VKELNLFDHK AHFSMEVIDT
KDFYPKKWEP AHLIHPAVLD VFVHLLISST GDAAEIKARV PVSTASLYIS ADFDSTSGTK
YHGFSTSKKH GATNMLSNVI AFAEGGSKPL IALEGCKTVP LRGASDPSSG DGQSLGHVPV
VPKKVVDVDI SDAVTLEKLL QGTDFASKLG SYLSLLGQKR PGLSVLEYSS STSSILLRAL
TAQAEELQGS ITSVALTTPL DGPADEETSV PEAWKNKVQQ EKLDLTQDPS TQGFEDVALD
VIFIDVEEQG DISLVLKNAK KILKPSGILL ITNHASAIST DLLTSTDLTS TTVSELIIAR
HKPDTDPSDH QVLIVTPPSP SSGLSKLIAQ AENDLTSQGY EVNKADFANI PEQTTPFLTL
SALDVDTPFL ESFHHETFTK LRSLFLASRG TLWLTLDTAS RGLVNGLGRT IRAEHPDISF
TVLSLDALTS LDSALNTKTI SSIIENMSRK TFGETSDSEY VIRNNQVLVE RLIPNPDLKA
LLDSSKTGNN LSAVKVPLKQ VNKPLQLSIR DPGLLDTLEY LSVPDLFEPL GDNQIEIEVG
SVGLNFRDVM VAMGQMEDNT LGIECAGVVA KVGAGVQKFK VGDRVFGMHA GCFQTRVRVD
PRTFQRTPEH LGDEEAASLM CTSATVVHSL IDVARLQRGE SVLIHSAAGG VGQAAIRLAK
YLGAEIFATV SSEKKKRLLI EDYGVKESHI FNSRDYSFAD GILRLTNQRG VDVVINSLAG
EALRRTWLCV APFGRFIELG KRDIYDNSGL DMRPFLDNIT FSGLDILTQV ISYPDRFEAI
GNQVVELLSK NAISPLNNLA RYSFGEVSKA FRLMQSGGHV GKIVLYPRPD DIVPIVPEGL
ESFCLPHDAT YVLIGGLGGI GRSVTRLLVE RGARHLVFLS RSAAARPEAQ ALLDELHAQG
VQAKAFAVDV AEKSQLEPVI NDVKQSFPAI KGLIHCAMDL RDAVYSNMTA DDWNASLRPK
LLATRNLHDL LPTDLDFFIC LSSIAGIIGS RGQANYNAGN TYQDALAHHR AASGLAATSI
NLSLVVGIGV STERSEVFQL LKDGGLLGMD ENDVLNVIKA AISGCAPTQV ALGASTGGQL
DKLAANDPYW FADSRFAVLN QLDRQGTGAV AGGQDWKKLL AAAASPDEVY EIVLQQLLEG
VSKIIKADVE DMDSRKSLPA LGIDSLVAIE IRTWLLKEFQ ADLSVFDIVS NDPLTGFAKK
VMAKSVLIA
