FUB8_FUSO4
ID FUB8_FUSO4 Reviewed; 1036 AA.
AC A0A0D2YG01;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Non-canonical non-ribosomal peptide synthetase FUB8 {ECO:0000303|PubMed:25372119};
DE EC=2.3.1.- {ECO:0000305|PubMed:25372119};
DE AltName: Full=Fusaric acid biosynthesis protein 8 {ECO:0000303|PubMed:25372119};
GN Name=FUB8 {ECO:0000303|PubMed:25372119}; ORFNames=FOXG_15239;
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: Non-canonical non-ribosomal peptide synthetase; part of the
CC gene cluster that mediates the biosynthesis of fusaric acid, a
CC mycotoxin with low to moderate toxicity to animals and humans, but with
CC high phytotoxic properties (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:S0DXJ2,
CC ECO:0000269|PubMed:25372119}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:25372119}.
CC -!- DOMAIN: Contains three distinct domains: an adenylation (A) domain that
CC activates the substrate amino acid which is subsequently covalently
CC linked as a thioester (aminoacyl-S-PCP) to the 4'-phosphopantetheine
CC prosthetic group of the second domain, the peptidyl carrier protein
CC (PCP) domain, as well as a thioester reductase (TR) release domain.
CC {ECO:0000250|UniProtKB:S0DXJ2}.
CC -!- DISRUPTION PHENOTYPE: Impairs 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; KNB17113.1; -; Genomic_DNA.
DR RefSeq; XP_018255158.1; XM_018395310.1.
DR AlphaFoldDB; A0A0D2YG01; -.
DR SMR; A0A0D2YG01; -.
DR EnsemblFungi; FOXG_15239T0; FOXG_15239P0; FOXG_15239.
DR EnsemblFungi; KNB17113; KNB17113; FOXG_15239.
DR GeneID; 28956315; -.
DR KEGG; fox:FOXG_15239; -.
DR VEuPathDB; FungiDB:FOXG_15239; -.
DR OMA; WVPAIID; -.
DR Proteomes; UP000009097; Chromosome 5.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 1: Evidence at protein level;
KW Multifunctional enzyme; NADP; Oxidoreductase; Phosphopantetheine;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..1036
FT /note="Non-canonical non-ribosomal peptide synthetase FUB8"
FT /id="PRO_0000437341"
FT DOMAIN 544..621
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 21..343
FT /note="Adenylation (A) domain"
FT /evidence="ECO:0000255"
FT REGION 658..899
FT /note="Thioester reductase (TR) domain"
FT /evidence="ECO:0000255"
FT MOD_RES 579
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1036 AA; 115084 MW; 35BD69CE65458C68 CRC64;
MGSISHLPAY GHRLLPVLID EIARDEPDRV LFYTPRNGQP SQGYDEVNTK IFANSINRLC
GWLDSQLGSP AGPRTIAYIG QNDLRYFIMM IASTKLGHRL LLSSPRNSVE GHVSLIKQSG
CEFWIASSGL DHHEFLQDLQ IPSVEAPELP QLLDPTPVKP YVYQKSWNEG KSDVLALLHT
SGSTGLPKLV PVYLETAATV DGFHLMEPTN GKRPTGVEWT GTRQLCAMPL FHVAGICLGL
YSAVFFNWTV VLPSVGPIMQ HVIEDALDHI SLDSAFISPS VLQDISKSPR VLEKLSKLKF
ITSAGGPIPQ SVGDLIHPRV PIMQTMGMTE GQWLASVVTH PDEWAYYYFH PRTGVEMRPY
SEDLSELVFV QNPKLSATQP VFKTFPELDI WETKDLYSRH PKHPDLWKYE MRRDDLIILS
NGEKFNPLAA EGKLISHPWI AAAYLTGRGR FQTAALLYPD ENSLDKSDDI ITDNVWPTFE
EVNKSLPAFA QIHRDFVKIV RTPFPRTPKG TLARNETEKA FTADINAIYD RSTHGKPSVH
INGTTEDVVR SGIREAIETV SGLVDLKDDD NIFTRGFDSL HVIRLAGLLS SAFDQPLEVE
AGTIYTNPTI SQLAHTVWSH LEHGPQDKVH HSEVTREMLA KYAQAFEPPR EAKEHIVLTG
TTGEIGSYLL DVLCNNDKVA KVWCLNRSAD AFQRQVDSAK SKGLSSSWKS KAKFVRYDVA
SENLGLSQDG LEEIKNEATA IIHNAWEVNF NLPLSSFEPQ FIGLKSLVDV CRESRQKIRF
FFVSSISAAM NWPSDLLGPV PEASIPRFDA PINGYGSSKL VAEHLLSKAA RSGVLSLSIL
RVGQVAGPVK TLGEGSIWTR RDWVPAIIDA SAHLRALPLD LGSASILDWI PIDLLTEVIG
QLVVPVNPVV GQENYYNLLN PRTPSWTDSL PGLKARLEAS FSDTFEIIPL QEWISRLRGA
EKTIVKEVSE GSSETAIRAQ SGLKLLAFFE MLASGKEGSR GLEWAKANTL AQSSFLACME
PVSSAWFDTW LKQWGY
