FUB3_GIBM7
ID FUB3_GIBM7 Reviewed; 510 AA.
AC W7MS01; W7NCM9;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Aspartate kinase FUB3 {ECO:0000303|PubMed:22652150};
DE EC=2.7.2.4 {ECO:0000305|PubMed:25372119};
DE AltName: Full=Fusaric acid biosynthesis protein 3 {ECO:0000303|PubMed:22652150};
GN Name=FUB3 {ECO:0000303|PubMed:22652150}; ORFNames=FVEG_12521;
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 FUNCTION.
RX PubMed=22652150; DOI=10.1016/j.fgb.2012.05.010;
RA Brown D.W., Butchko R.A., Busman M., Proctor R.H.;
RT "Identification of gene clusters associated with fusaric acid, fusarin, and
RT perithecial pigment production in Fusarium verticillioides.";
RL Fungal Genet. Biol. 49:521-532(2012).
RN [7]
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 [8]
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 [9]
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 [10]
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 [11]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, 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: Aspartate kinase; 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:22652150, PubMed:25372119). L-aspartate is suggested as fusaric
CC acid amino acid precursor that is activated and further processed to O-
CC acetyl-L-homoserine by cluster enzymes aspartate kinase FUB3 and
CC homoserine O-acetyltransferase FUB5, as well as enzymes of the primary
CC 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:S0DVT6,
CC ECO:0000269|PubMed:22652150, ECO:0000269|PubMed:25372119}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-aspartate = 4-phospho-L-aspartate + ADP;
CC Xref=Rhea:RHEA:23776, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57535, ChEBI:CHEBI:456216; EC=2.7.2.4;
CC Evidence={ECO:0000305|PubMed:22652150};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:22652150,
CC 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 -!- DISRUPTION PHENOTYPE: Strongly reduces production of fusaric acid
CC (PubMed:25372119). {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 aspartokinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EWG54262.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DS022261; EWG54263.1; -; Genomic_DNA.
DR EMBL; DS022261; EWG54262.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_018760453.1; XM_018901861.1.
DR RefSeq; XP_018760454.1; XM_018901862.1.
DR AlphaFoldDB; W7MS01; -.
DR SMR; W7MS01; -.
DR STRING; 117187.FVEG_12521T0; -.
DR EnsemblFungi; FVEG_12521T0; FVEG_12521T0; FVEG_12521.
DR GeneID; 30069955; -.
DR KEGG; fvr:FVEG_12521; -.
DR VEuPathDB; FungiDB:FVEG_12521; -.
DR eggNOG; KOG0456; Eukaryota.
DR HOGENOM; CLU_009116_6_4_1; -.
DR OMA; IIQSQRC; -.
DR OrthoDB; 113181at2759; -.
DR PHI-base; PHI:3389; -.
DR Proteomes; UP000009096; Chromosome 3.
DR GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1160.10; -; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR005260; Asp_kin_monofn.
DR InterPro; IPR001341; Asp_kinase.
DR InterPro; IPR018042; Aspartate_kinase_CS.
DR InterPro; IPR027795; CASTOR_ACT_dom.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF13840; ACT_7; 1.
DR PIRSF; PIRSF000726; Asp_kin; 1.
DR SUPFAM; SSF53633; SSF53633; 1.
DR SUPFAM; SSF55021; SSF55021; 2.
DR TIGRFAMs; TIGR00657; asp_kinases; 1.
DR PROSITE; PS51671; ACT; 2.
DR PROSITE; PS00324; ASPARTOKINASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transferase.
FT CHAIN 1..510
FT /note="Aspartate kinase FUB3"
FT /id="PRO_0000437313"
FT DOMAIN 372..440
FT /note="ACT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT DOMAIN 446..510
FT /note="ACT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
SQ SEQUENCE 510 AA; 56004 MW; F869711002C80A9C CRC64;
MRSRRDNSWV VQKFGGTSIG KFPDKVAEIV KSARLGGDRP AVICSARSSG KKVFGTTSRL
LQVYRTLRGI VAITQDPDMQ ELLFDRLRSI IKDIRDDQVA TVQIYILRQD IRDETTRQIT
ADCQELLDYT SAAKRFNLDI NGKAKDKMVS FGEKLSCRLM VAMLRDRDIP AEYVDLSDIV
PNNNLNHLKP EFFPEAAAVF GKRIEACNGR VPVITGFFGA VPGSLIDSGI GRGYSDLCAV
LVAIGLHAER VQIWKEVDGI FTADPREVPD ARCLPSITPS EAAELTFYGS EVIHHLALSL
AIQAKPPISI FVKNVQKPWG QGTVVVPSDG DDTSSWPIDY LDPSDSDCTS STALPKMPTA
VTIKRDITIL NILSNKQSMS HGFFVKVFTI LAEHDISVDL ISTSEVHVSM AINSSNMDPS
QIKDVHCKIA EEGEVNVLPD MAILSLVGAE LKNMTGIAGR MFAILGEQHV NIEMISQGAS
EINISCVIPD KDATRALNML HNELFTKNAM
