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FUB8_GIBM7
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   03-AUG-2022, entry version 31.
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; 117187.FVEG_12530T0; -.
DR   GeneID; 30069963; -.
DR   KEGG; fvr:FVEG_12530; -.
DR   VEuPathDB; FungiDB:FVEG_12530; -.
DR   eggNOG; KOG1178; Eukaryota.
DR   OrthoDB; 229565at2759; -.
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: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; IPR009081; PP-bd_ACP.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF00550; PP-binding; 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..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
 
 
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