FUB9_GIBF5
ID FUB9_GIBF5 Reviewed; 358 AA.
AC S0DRI9;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Oxidase FUB9 {ECO:0000303|PubMed:26662839};
DE EC=1.-.-.- {ECO:0000305|PubMed:26662839};
DE AltName: Full=Fusaric acid biosynthesis protein 9 {ECO:0000303|PubMed:26662839};
GN Name=FUB9 {ECO:0000303|PubMed:26662839}; ORFNames=FFUJ_02116;
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, 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: 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:26662839). 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 (PubMed:26662839). 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 (PubMed:26662839). FUB1, FUB4, and
CC 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 -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00683};
CC -!- PATHWAY: Mycotoxin biosynthesis. {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}.
CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; HF679025; CCT65194.1; -; Genomic_DNA.
DR AlphaFoldDB; S0DRI9; -.
DR SMR; S0DRI9; -.
DR STRING; 1279085.S0DRI9; -.
DR EnsemblFungi; CCT65194; CCT65194; FFUJ_02116.
DR VEuPathDB; FungiDB:FFUJ_02116; -.
DR HOGENOM; CLU_020639_0_0_1; -.
DR Proteomes; UP000016800; Chromosome 3.
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 Flavoprotein; FMN; Oxidoreductase; Reference proteome.
FT CHAIN 1..358
FT /note="Oxidase FUB9"
FT /id="PRO_0000437348"
FT DOMAIN 6..350
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT ACT_SITE 245
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 32
FT /ligand="a 2-oxocarboxylate"
FT /ligand_id="ChEBI:CHEBI:35179"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 114
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 138
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 166
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 175
FT /ligand="a 2-oxocarboxylate"
FT /ligand_id="ChEBI:CHEBI:35179"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 221
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 248
FT /ligand="a 2-oxocarboxylate"
FT /ligand_id="ChEBI:CHEBI:35179"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 276..280
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 299..300
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
SQ SEQUENCE 358 AA; 38314 MW; BCB950522C2F7451 CRC64;
MSDATSSKPQ IFSIQDLKQA ASDKMSQMYR DYYNGGAMDN ITLANNEAAF DRYLLRPRVL
RNVSNIDMTT TLWGTKAALP LGVSPSAMHR LAHADGEVGT SKACAARHVP MILSALSNDT
LEDVSGQSSD GSTPYAIQVS PFKNRQITTN LLNRAKAAGY KAVVLTVDAP MFGRRLDDLR
NGFSSGGLGG GIPDLSFDTS ATWEEKIAWM KSQTDLEIWV KGVTSPLDAQ IAIEQGVDGI
IISNHGGRQL DTTPATIDIL REIAPIAKGK TRIAIDGGFR RGSDIFKAVA LGADFVFVGR
IAIWGLAYDG SNGVGLALDL LINEFKLCMG LAGCSKISDI SPAHLSILNA RGVLESVY
