FUB1_GIBF5
ID FUB1_GIBF5 Reviewed; 2410 AA.
AC S0DRI1;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Reducing polyketide synthase FUB1 {ECO:0000303|PubMed:24389666};
DE EC=2.3.1.- {ECO:0000305|PubMed:26662839};
DE AltName: Full=Fusaric acid biosynthesis protein 1 {ECO:0000303|PubMed:24389666};
GN Name=FUB1 {ECO:0000303|PubMed:24389666}; ORFNames=FFUJ_02105;
OS Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS and foot rot disease fungus) (Fusarium fujikuroi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1279085;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831;
RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA Wiemann P., Sieber C.M.K., von Bargen K.W., Studt L., Niehaus E.-M.,
RA Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA Proctor R.H., Muensterkoetter M., Freitag M., Humpf H.-U., Gueldener U.,
RA Tudzynski B.;
RT "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT novel metabolites.";
RL PLoS Pathog. 9:E1003475-E1003475(2013).
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 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 [7]
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 [8]
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 [9]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=24389666; DOI=10.1007/s00253-013-5453-1;
RA Niehaus E.M., von Bargen K.W., Espino J.J., Pfannmueller A., Humpf H.U.,
RA Tudzynski B.;
RT "Characterization of the fusaric acid gene cluster in Fusarium fujikuroi.";
RL Appl. Microbiol. Biotechnol. 98:1749-1762(2014).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RX PubMed=26662839; DOI=10.1111/1462-2920.13150;
RA Studt L., Janevska S., Niehaus E.M., Burkhardt I., Arndt B., Sieber C.M.,
RA Humpf H.U., Dickschat J.S., Tudzynski B.;
RT "Two separate key enzymes and two pathway-specific transcription factors
RT are involved in fusaric acid biosynthesis in Fusarium fujikuroi.";
RL Environ. Microbiol. 18:936-956(2016).
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:24389666, PubMed:26662839). 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 (PubMed:26662839). The polyketide synthase (PKS)
CC FUB1 generates the triketide trans-2-hexenal which is presumptively
CC released by the hydrolase FUB4 and linked to the NRPS-bound amino acid
CC precursor by NAD(P)-dependent dehydrogenase FUB6 (PubMed:26662839).
CC FUB1, FUB4, and the non-canonical NRPS Fub8 may form an enzyme complex
CC (PubMed:26662839). Further processing of the NRPS-bound intermediate
CC might be carried out by FUB6 and the sulfhydrylase FUB7, enabling a
CC spontaneous electrocyclization to close the carbon backbone of fusaric
CC acid (PubMed:26662839). Dihydrofusaric acid is likely to be released
CC via reduction by the thioester reductase (TR) domain of FUB8 whereupon
CC the final oxidation to fusaric acid may (also) be performed by the FMN-
CC dependent dehydrogenase FUB9 (PubMed:26662839).
CC {ECO:0000269|PubMed:24389666, ECO:0000269|PubMed:26662839}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:26662839}.
CC -!- INDUCTION: Expressed under high amounts of nitrogen via regulation by
CC AREB (PubMed:24389666). Moreover, components of the fungal-specific
CC velvet complex VEL1 and LAE1 act also as positive regulators of
CC expression (PubMed:24389666). Finally, the pH regulator PACC acts as
CC activator of FUB expression after the pH shift to alkaline ambient
CC conditions (PubMed:24389666). {ECO:0000269|PubMed:24389666}.
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:24389666, PubMed:26662839). {ECO:0000269|PubMed:24389666,
CC ECO:0000269|PubMed:26662839}.
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; HF679025; CCT65184.1; -; Genomic_DNA.
DR AlphaFoldDB; S0DRI1; -.
DR SMR; S0DRI1; -.
DR STRING; 1279085.S0DRI1; -.
DR EnsemblFungi; CCT65184; CCT65184; FFUJ_02105.
DR VEuPathDB; FungiDB:FFUJ_02105; -.
DR HOGENOM; CLU_000022_31_0_1; -.
DR BioCyc; MetaCyc:MON-19342; -.
DR Proteomes; UP000016800; 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 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_0000437307"
FT DOMAIN 2329..2406
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 1..52
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..38
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; 259533 MW; FBA989E0F29DD422 CRC64;
MTLSNGSNGA NGTSNGNGAH PSANGFHNAA NGGANNGSAN GGAEHDAGRP 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 SAGLSFDKTN
LFEAHGTGTK VGDPIECSVI GNVFGKTREK PVYVGSVKSN IGHLEGASGL AGLVKTIYSL
ESGVISPTYG LEHVNPKIKL DEWKINIPTE EIKWPAGLRR ASINSFGYGG ANAHAVLDDA
YHFLKTHNLK GHHNTKVEGV LNTGLIANGS QDVIEGTDKK SHLFLLSSHE ESGIARLSQT
LQAYLAETSA RKLPEDQFLH RLAYTLSEKR SALPWKTYAA ASTIEELQQA LDGAPAKAAR
VPRSQALTFI FTGQGAQWFA MGRELQKYPV FQQSLHACSQ YLKDFGSTWD LVEELNRDAK
ESIIDLPYVS QPSCTALQLS IIDLLASWGI HPQVTVGHSS GEIAAAYAKG AFDKEAAMRI
AYFRGHLTGN ITKTGSMAAV GLGPDRVSEY MSRVTAGKIV IACINSPASV TLSGDVEGID
EVLTFLQADD IFARKLRVTT AYHSHHMQQI SEEYLNSLSG KWELKPGNPK VRMFSSVSAK
AIDGTELGPA YWVANLVSPV NFSGAVTAAA NAGALGKRKT SGKKGSADAM VEIGPHAALQ
GPLKQILDSI GDKGASPKYF SAIKRKQDAI QTTLEVVGEL LVLGHQVNIP LANTYTETTS
ALVDLPPYAW NTANSYWHES AAVTAYKQRK HPRLELLGVR DPRSTKAEPA WHNYLRISEQ
PWIEHHQFQN TNIYPMAGMI VMAIEGLRQV ETRADVEGYT IRDVNIGSAL VVPPDQTVET
RLQLTPWRSG PNVSWSHWTE FTVSSRNESG SWTTNCTGLV STSYKHDTNS TFLDEEAAAN
ALLNQEYKDI SKSDLPSVDP TVFYTKLDES GFSLGPAFRG VKELNLFDHK AHFSMEVIDT
KEFYPKKWEP AHLIHPAVLD VFVHLLISST GDAAEIKARV PVSTASLYIS ADFDSTGGTK
YHGFSTSKKH GATNMLSDVI AFAEGGSKAL IALKGCKTVP LRGASDSSSG DGQPLGHVPV
VPKKVVDVEI SDAATLGQLL TGTDLASKLA SYLSLLGQKR PGLRVLEYSS STSSTLLKAL
TAQAEDLQGS LSSVALTTPL DGPADELTSV PETWKNKVRQ EKLDLAQDPS TQGFEDVALD
VIILDVEDQQ GDISLVLKNA KKVLKPSGIL LIANHTAAIS TDLLTSTGFT STTVSDLIIA
RHKPETEPPV RRVLVVTPST TSPGLGRLIT QAESDLTSRG YEVAKTDFGS IPEQATPFLT
LSALDIDAPF LEGFHHETFA KLRSLFLASR GTLWLTLDTA SRGLVNGLGR TIRAEHPDIS
FTTLGLDASA ALDSASNTKT ISSIIDNISR KTFGETSDSE YVIRDNQVLI ERLIPNPGLK
ALLDSSKTGN KLSAVKIPLK QVAKPLQLSI RDHGLLDTLE YLSVPDLPEP LGDNQIEIEV
GSVGLNFRDV MVAMGQMEDS TLGIECAGVV VKVGAGVQKF KVGDRVFGMH AGCFQTRVRV
DPRTFQRTPD NLGDEEAASL MCTSATVVHS LIDVARLQRG ESVLIHSAAG GVGQTAIRLA
KHLGAEIFAT VSSEKKKRLL VEEYGIKESH IFNSRDYSFA DGILRLTNQR GVDVVINSLA
GEALRRTWLC VAPFGRFIEL GKRDIYDNSG LDMRPFLDNI TFSGLDILTQ VISYPDRFEA
IGNQVVELLS KNAISPLNNL ARYSFGEVSK AFRLMQSGGH VGKIVLYPRP DDIVPVVPDG
LESFCLPHDA TYVLIGGLGG IGRSVTRLLV QRGARHLVFL SRSAASRPEA QALLDEVHAQ
GVQAKAFAVD VAEKSQLEPV INDVKQSFPA IKGLIHCAMD LRDAVYSNMT ADDWNASLRP
KLLATRNLHD LLPTDLDFFI CLSSIAGIIG SRGQANYNAG NTYQDALAHQ RAASGLAATS
INLSLVVGIG VSTERSEVFQ LLKDGGLLGM DENDVLNIIK AAISGRTPTQ VALGASTGGQ
LDKLAANDPY WFADSRFAVL NQLDRQGTGA VAGGQDWKKL IAAAASPDEV YEIVLQQLLE
GVSKIIKADV EDMDSRRSLP ALGIDSLVAI EIRTWLLKEF QADLSVFDIV SNDPLTGFTK
KVMAKSALIA
