FUB1_FUSO4
ID FUB1_FUSO4 Reviewed; 2410 AA.
AC A0A0D2YG10; A0A0J9WU41;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2016, sequence version 2.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Reducing polyketide synthase FUB1 {ECO:0000303|PubMed:25372119};
DE EC=2.3.1.- {ECO:0000305|PubMed:25372119};
DE AltName: Full=Fusaric acid biosynthesis protein 1 {ECO:0000303|PubMed:25372119};
GN Name=FUB1 {ECO:0000303|PubMed:25372119}; ORFNames=FOXG_15248;
OS Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935
OS / NRRL 34936) (Fusarium vascular wilt of tomato).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=426428;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4287 / CBS 123668 / FGSC 9935 / NRRL 34936;
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 IDENTIFICATION.
RC STRAIN=4287 / CBS 123668 / FGSC 9935 / NRRL 34936;
RG EnsemblFungi;
RL Submitted (MAR-2015) to UniProtKB.
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
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:25372119). L-aspartate is suggested as fusaric acid
CC amino acid precursor that is activated and further processed to O-
CC acetyl-L-homoserine by cluster enzymes aspartate kinase FUB3 and
CC homoserine O-acetyltransferase FUB5, as well as enzymes of the primary
CC 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:25372119}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {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: Reduces to 5% the production of fusaric acid
CC (PubMed:25372119). {ECO:0000269|PubMed:25372119}.
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; DS231721; KNB17122.1; -; Genomic_DNA.
DR RefSeq; XP_018255167.1; XM_018395332.1.
DR AlphaFoldDB; A0A0D2YG10; -.
DR SMR; A0A0D2YG10; -.
DR STRING; 426428.A0A0D2YG10; -.
DR EnsemblFungi; KNB17122; KNB17122; FOXG_15248.
DR GeneID; 28956322; -.
DR KEGG; fox:FOXG_15248; -.
DR VEuPathDB; FungiDB:FOXG_15248; -.
DR BioCyc; MetaCyc:MON-19346; -.
DR PHI-base; PHI:6936; -.
DR Proteomes; UP000009097; Unplaced.
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 Gene3D; 3.40.50.150; -; 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; IPR029063; SAM-dependent_MTases_sf.
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; SSF53335; SSF53335; 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..2410
FT /note="Reducing polyketide synthase FUB1"
FT /id="PRO_0000437309"
FT DOMAIN 2329..2406
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 1..50
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 1714..2026
FT /note="Enoyl reductase (ER) domain"
FT /evidence="ECO:0000255"
FT REGION 2050..2226
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..42
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 2366
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2410 AA; 260094 MW; 005B257306E4B43D CRC64;
MTLFNGSNGA NGTSSGHGAH PSANGFHNAA NGGANNGTAN GGVEHDASLP QVDGDISSAI
AVIGVSGRFP GDGTSPRHLW DLLKEGRNAL SDVPESRFNI DGFYHPDGGR AGTLNTKQGY
FLQSDVDKFD AGFFSITPEE ARGMDPTQRI LLELAYEGLE NAGLKIDEVA NQHMSCYIGA
CQHDYWDLQA YDMDSAPKYT ATGTGPALLS NRISWFFNLK GPSVTIDTAC SSTLTALHLA
GQSIRNGESD SALVGGLGLH LLPNFGVFMS SMSFLSADNK CHSFDASANG YARAEGGGFV
VLKRLDKALS DGDTIRAVLR STGSNQDGRT LGITQPSASR QEELIRATYA SAGLSFDKTN
FFEAHGTGTK VGDPIECSVI GNVFGKTREK PVYVGSVKSN IGHLEGASGL AGLVKTIYSL
ESGVISPTYG LENVNPKIKL DEWKINIPTE EIKWPAGLRR ASINSFGYGG ANAHAVLDDA
YHFLKTHNLK GHHNTKVEGV LTTGLIGNGS QDASDKTDKK SRLFLLSSHE ESGIARLSQT
LQAYLTEPAA RELPEDQFLH RLAYTLSEKR SSLPWKTYAA ASTIEELQQA LDGAPTKAAR
VPRPQALTFI FTGQGAQWFA MGRELQKYPV FQQSLHACSQ YLKDFGSTWD LVEELNRDAK
ESIIDLPYVS QPSCTALQLS IIDLLASWGI HPQVTIGHSS GEIAAAYAKG AFDKEAAMRI
AYFRGHLTGN ITKTGSMAAV GLGPERVSEY LSRVTAGKIV IACINSPASV TLSGDVEGID
EVLTFLQADD IFARKLRVTT AYHSHHMQQI SEEYLNSLSG KWELKPGNPK VRMFSSVSAK
PIDGTELGPA YWVANLVSPV NFSGAVTAAA NAGALGKRKA SGKKGSADAM VEIGPHAALQ
GPLKQILDSI GDKGASPKYF SAIKRKQDAI QTTLEVVGEL LVLGHPVNVP LANAYTETTS
ALVDLPPYAW NTTNSYWHES AAVTAYKQRK HPRLELLGVR DPRSTKAEPA WHNYLRISEQ
PWIEHHQFQN TNIYPMAGMI VMAIEGLRQV ETRTDVEGYT IRDVNIGSAL VVPLDQTVET
RLQLTPWRSG PNVSWSHWTE FTVSSRNESG SWTTNCTGLV STSYKHETNS TFLDEEAAAN
ALLNQEYKDI SQSDLPSVDP TVFYTKLDES GFSLGPAFRG VKQLNLFDHK AHFSMEVIDT
KEFYPKKWEP AHLIHPAVLD VFVHLLISST GDAAEIKARV PVSTASLYIS ADFDSTSGTK
YHGFSTSKKH GATNMLSDVI AFAENGTKPL IALKGCKTVP LRGASDSSSG DGQSLGHVPV
VPKKVVDIEI SDAVTLEQLL RGTDLASKLG SYLSLLGQKL PGLNVLEYSS STSSTLLKAL
TAQAEELQGS IASVTLTTPL DGPVDVEASV PEAWKNKIQQ EKLDLAQDPS SQGYEDATLD
VIFLDVEEQQ GDISLILKNA KKILKPSGIL LIANHAAAIS TDLFSSSSFI STSVSDLIIA
RHKPETEPSV RRVLIVTPSS PSSGLSQLVA QAESDLTSQG YEVAKTDFAN IPEQTTPFLT
LSTLDIDTPF LENFDHETFT KLRSLFLASR GTLWLTLDTA SRGLVNGLGR TIRAEHPDIS
FTTLGLDAST SLDSALNTKT ISTIVENISR KIFGETSDSE YVIRNNQVLV ERLIPNPDLK
ALLDSSKTGN NLSAVKMPLK QVIKPLQLSI RDPGLLDTLE YLSVPDLSGP LGDNQIEIEV
GSVGLNFRDV MVAMGQMEDN TLGIECAGVV SKVGAGVQKF KVGDRVFGMH AGCFQTRVRV
DPRTFQRTPD HLGDEEAASL MCTSATVVHS LIDVARLQRG ESVLIHSAAG GVGQTAIRLA
KYLGAEIFAT VSSEKKKRLL IEEYGIKESH IFNSRDYSFA DGVLRLTNQR GVDVVINSLA
GEALRRTWLC VAPFGRFIEL GKRDIYDNSG LDMRPFLDNI TFSGLDILTQ VISYPDRFEA
IGSQVVELLS KNAISPLNNL ARYSFGEVSK AFRLMQSGGH VGKIVLYPRP DDIVPVVPEG
LESFCLPHDA TYVLIGGLGG IGRSVTRLLV ERGARHLIFL SRSAASRPEA QALLDELHAQ
GVQAKAFAVD VAEKSQLEPV INGVKQSFPA IKGLIHCAMD LRDAVYSNMT ADDWNASLRP
KLLATRNLHE LLPTDLDFFI CLSSIAGIIG SRGQANYNAG NTYQDALAHH RAASGLAATS
INLSLVVGIG VSTERSEVFQ LLKDGGLLGM DENDVLNVIK AAISGRTPTQ VALGASTGGQ
LDKLAANDPY WFADSRFAVL NQLDRQGTGA TAGGQDWKKL LAAAASPDEV YEIVLQQLLE
GVSKIIKADV EDMDSRKSLP ALGIDSLVAI EIRTWLLKEF QADLSVFDIV SNDPLTGFAK
KVMAKSALIA
