ID FUB8_GIBM7 Reviewed; 1058 AA.
AC W7N2C1;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=FVEG_12530;
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 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 [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, 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: 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 -!- 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: 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 -!- 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; EWG54274.1; -; Genomic_DNA.
DR RefSeq; XP_018760465.1; XM_018901870.1.
DR AlphaFoldDB; W7N2C1; -.
DR SMR; W7N2C1; -.
DR STRING; 334819.W7N2C1; -.
DR GeneID; 30069963; -.
DR KEGG; fvr:FVEG_12530; -.
DR VEuPathDB; FungiDB:FVEG_12530; -.
DR eggNOG; KOG1178; Eukaryota.
DR OrthoDB; 2230730at2759; -.
DR PHI-base; PHI:3384; -.
DR Proteomes; UP000009096; Chromosome 3.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR PANTHER; PTHR43439:SF2; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR PANTHER; PTHR43439; PHENYLACETATE-COENZYME A LIGASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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..1058
FT /note="Non-canonical non-ribosomal peptide synthetase FUB8"
FT /id="PRO_0000437340"
FT DOMAIN 566..643
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 43..365
FT /note="Adenylation (A) domain"
FT /evidence="ECO:0000255"
FT REGION 680..921
FT /note="Thioester reductase (TR) domain"
FT /evidence="ECO:0000255"
FT MOD_RES 601
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1058 AA; 117641 MW; 870997DF90E41612 CRC64;
MQKIAKQALS SLSSLAKSPA NAMGSISHLP AYGHRLLPVL IDEISRDEPD RVLFYTPRNG
QPSQGYDEVT TKIFANAIDR LCGWLDSQLG SPTVSKTIAY IGQNDLRYFI IMIASTKLGH
RLLLSSPRNS VEGHVSLIKQ SGCELWIASS GLGHHEFLQD LHIPSVEAPE LSELLDPTLA
KPYIYQKSWH EGKSDVLALL HTSGSTGLPK LVPVYLETAA TVDGFHLMEP TDGKRPTGVE
WTGTRQLCAM PLFHVAGICL GLYSAVFFNW IVVLPSVGPI MQHVIEDALD HISLDSAFIS
PSVLQDISKS SRVLEKLSKL KFITSAGGPI PQSVGDLIHP RVPIMQTMGM TEGQWLASVV
MHPDEWAYYY FHPRTGVEMR PYSEDLFELV FVQNPKLSAT QPVFKTFPDL DIWETKDLYS
RHPKHPDLWK YEMRRDDLII LSNGEKFNPL AAEGKLISHP WIAAAYLTGR GRFQTAALIY
PDDSSFNNSD DTIIDNIWPT FEEVNKSLPA FAQIHRDFVK IVRTPFPCTP KGTLARNETE
KSFNADINAI YDRSTHGKPS VHINGTTEDV VRSGIREAIE TVSGLVDLKD DDNIFTRGFD
SLHVIRLAGL LSSAFYQPLE VEPGTIYTNP TISQLSHSVW THLEYGPQDR IHHSEVTLEM
LAKYIQAFEP PRESKEHIVL TGTTGEIGSY LLDDICKNDK VAKVWCLNRS VDAFQRQVDS
AKSKGLSSNW QSKAKFVRYD VTSENLGLSQ DDLEEIKNEA TAIIHNAWEV NFNLPLSSFD
PQFVGLQGLV DVCRATRHKI RFFFVSSISA AMNWPSDLLG PVPEASISRF DAPINGYGSS
KLVAEHLLSK AARSGVLSLS VLRVGQVAGP VRTLGEGSIW TRRDWVPAII DASVHLRALP
LDLGSASILD WIPIDLLAEV IGQLVVPVNP VVGQENYYNL LNPRTPSWKD TLPGLKAHLE
ASFSEKFEII PLQEWINRMR GAEKTIVKEV SEGSSETARR AQSGLKLLAF FETLASETEG
SRGLEWSKAN ALAQSSILAC MEPVSSAWFD TWLTQWGY
//
