FUB8_GIBF5
ID FUB8_GIBF5 Reviewed; 1036 AA.
AC S0DXJ2;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Non-canonical non-ribosomal peptide synthetase FUB8 {ECO:0000303|PubMed:26662839};
DE EC=2.3.1.- {ECO:0000305|PubMed:26662839};
DE AltName: Full=Fusaric acid biosynthesis protein 8 {ECO:0000303|PubMed:26662839};
GN Name=FUB8 {ECO:0000303|PubMed:26662839};
GN Synonyms=NRPS34 {ECO:0000303|PubMed:26662839}; ORFNames=FFUJ_02115;
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, DOMAIN, 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: 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: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:26662839}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:26662839}.
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:0000305|PubMed:26662839}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of fusaric acid
CC (PubMed:26662839). {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; CCT65193.1; -; Genomic_DNA.
DR AlphaFoldDB; S0DXJ2; -.
DR SMR; S0DXJ2; -.
DR STRING; 5127.CCT65193; -.
DR EnsemblFungi; CCT65193; CCT65193; FFUJ_02115.
DR VEuPathDB; FungiDB:FFUJ_02115; -.
DR HOGENOM; CLU_002220_0_0_1; -.
DR Proteomes; UP000016800; Chromosome 3.
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_0000437339"
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; 115068 MW; 31C7FFF763B4B490 CRC64;
MGSISHLPVY GHRLLPVVID EIARDEPDRV LFYTPRNGQP SQGYDKVTTK IFANSINRLC
GWLDSQLGSP TVSKTIAYIG QNDLRYFIMM IASTKLGHRL LLSSPRNSVE GHVSLIKQSG
CEFWIASSGL DHHGFLQDLQ IPSVEAPELS QLLDPTPLKP YVYQKSWNEG KSDILALLHT
SGSTGLPKLV PVYLETAATV DGFHLMELTN GKRPTGVEWT GTRQLCAMPL FHVAGICLGL
YSAVFFNWTV VLPSVGPIMQ HVIEDALDHI TLDSAFISPS VLQDISKSPR VLEKLSKLKF
ITSAGGPIPQ SVGDLIHPRV PIMQTMGMTE GQWLASVVTH PDEWAYYYFH PRTGVEMRPY
SEDLSELVFV QNPKLTATQP VFKTFPELDI WETKDLYSRH PKHPSLWKYE MRRDDLVILS
NGEKFNPLAA EGKLISHPWI AAAYLTGRGR FQTAALLYPD ETNLDKSDDT IIDNVWPTFE
EVNRSLPAFA QIHRDFVKIV RTPFPRTPKG TLARNETEKA FTADINAIYD RSTHGKPSVH
INGTTEVVVR SGIREAIEAV SGLVDLKDDD NIFTRGFDSL HVIRLAGLLS SAFDQPIEVE
VGTIYTNPTV SQLARSVWSH LEHGPQDKIH HSEATREMLA KYAQAFEPPR EAKEHIVITG
TTGEIGSYLL DVLCNNDKVA KIWCLNRSAD AFQRQVDSAK SKGLSSTWQS KAKFVRYDVA
ADNLGLSQDD LQEIKNQATA IIHNAWEVNF NLPLSSFEPQ FVGLQSLVDI CREARHKLRF
FFISSISAAM NWPSDLLGPV PEASIPRFDA PINGYGSSKL VAEHLLSKAA RSGVLSLSVL
RVGQVAGPVK TLGEGSIWTR RDWVPAIIDA SVHLRALPLD LGTASILDWI PIDLLTEVIG
QLVVPVNAVV GQENYYNLLN PRTPSWIDAL PGLKAHLEVS FSDKFEIIPL HEWIGRLRGA
EKTIVKEVSE GSSETARRAQ SGLKLLAFFE MLASGEEGSR GLEWSKGNTL AQSSILACME
PVSSAWFGTW LTQWGY
