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FUB9_FUSO4
ID   FUB9_FUSO4              Reviewed;         387 AA.
AC   A0A0D2YG00; A0A0J9W2J1;
DT   05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2016, sequence version 2.
DT   03-AUG-2022, entry version 27.
DE   RecName: Full=Oxidase FUB9 {ECO:0000303|PubMed:25372119};
DE            EC=1.-.-.- {ECO:0000305|PubMed:25372119};
DE   AltName: Full=Fusaric acid biosynthesis protein 9 {ECO:0000303|PubMed:25372119};
GN   Name=FUB8 {ECO:0000303|PubMed:25372119}; ORFNames=FOXG_15238;
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, 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: Oxidase; part of the gene cluster that mediates the
CC       biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity
CC       to animals and humans, but with high phytotoxic properties
CC       (PubMed:25372119). L-aspartate is suggested as fusaric acid amino acid
CC       precursor that is activated and further processed to O-acetyl-L-
CC       homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O-
CC       acetyltransferase FUB5, as well as enzymes of the primary metabolism
CC       (By similarity). The polyketide synthase (PKS) FUB1 generates the
CC       triketide trans-2-hexenal which is presumptively released by the
CC       hydrolase FUB4 and linked to the NRPS-bound amino acid precursor by
CC       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:S0DRI9,
CC       ECO:0000269|PubMed:25372119}.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00683};
CC   -!- PATHWAY: Mycotoxin biosynthesis. {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}.
CC   -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; DS231721; KNB17095.1; -; Genomic_DNA.
DR   RefSeq; XP_018255140.1; XM_018395307.1.
DR   AlphaFoldDB; A0A0D2YG00; -.
DR   SMR; A0A0D2YG00; -.
DR   STRING; 426428.A0A0D2YG00; -.
DR   EnsemblFungi; KNB17095; KNB17095; FOXG_15238.
DR   GeneID; 28956314; -.
DR   KEGG; fox:FOXG_15238; -.
DR   VEuPathDB; FungiDB:FOXG_15238; -.
DR   Proteomes; UP000009097; Unplaced.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR012133; Alpha-hydoxy_acid_DH_FMN.
DR   InterPro; IPR000262; FMN-dep_DH.
DR   InterPro; IPR037396; FMN_HAD.
DR   InterPro; IPR008259; FMN_hydac_DH_AS.
DR   Pfam; PF01070; FMN_dh; 1.
DR   PIRSF; PIRSF000138; Al-hdrx_acd_dh; 1.
DR   PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1.
DR   PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE   1: Evidence at protein level;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..387
FT                   /note="Oxidase FUB9"
FT                   /id="PRO_0000437350"
FT   DOMAIN          18..379
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        274
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   BINDING         44
FT                   /ligand="a 2-oxocarboxylate"
FT                   /ligand_id="ChEBI:CHEBI:35179"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   BINDING         126
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   BINDING         150
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   BINDING         178
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   BINDING         187
FT                   /ligand="a 2-oxocarboxylate"
FT                   /ligand_id="ChEBI:CHEBI:35179"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   BINDING         250
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   BINDING         277
FT                   /ligand="a 2-oxocarboxylate"
FT                   /ligand_id="ChEBI:CHEBI:35179"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   BINDING         305..309
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   BINDING         328..329
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
SQ   SEQUENCE   387 AA;  41274 MW;  61490D5830918C28 CRC64;
     MSRTNLPIQP AKMSDATSSK PQIFSIQDLK QAASDKMSQM YRDYYNGGAM DNITLASNEA
     AFDRYLLRPR VLRNVSNIDM TTTLWGTKAA LPLGVSPSAM HRLAHADGEV GTSKACAARN
     VPMILSALSN DTLEDVSGQS SDGSTPYAIQ VSPFKNRQIT TNLLSRAKAA GYKAVVLTVD
     APMFGRRLDD LRNGFSIPPG FSFPNLSAQT QSGSGGLGGG IPDLSFDTAA TWEEKIAWMK
     SQTDLEIWVK GVTSPLDAQI AIEQGVDGII ISNHGGRQLD TTPATIDILR EIAPIAKGKT
     RIAIDGGFRR GSDIFKAVAL GADFVFVGRI AIWGLAYDGS NGVGLALDLL INEFKLCMGL
     AGCSKISDIT PAHLSILNAK GVLESVY
 
 
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