FUB3_FUSO4
ID FUB3_FUSO4 Reviewed; 542 AA.
AC A0A0D2YG09;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Aspartate kinase FUB3 {ECO:0000303|PubMed:25372119};
DE EC=2.7.2.4 {ECO:0000305|PubMed:25372119};
DE AltName: Full=Fusaric acid biosynthesis protein 3 {ECO:0000303|PubMed:25372119};
GN Name=FUB3 {ECO:0000303|PubMed:25372119}; ORFNames=FOXG_15247;
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, DISRUPTION PHENOTYPE, 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: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:S0DVT6,
CC 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:25372119};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:25372119}.
CC -!- DISRUPTION PHENOTYPE: Impairs the 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}.
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DR EMBL; DS231721; KNB17121.1; -; Genomic_DNA.
DR RefSeq; XP_018255166.1; XM_018395331.1.
DR AlphaFoldDB; A0A0D2YG09; -.
DR SMR; A0A0D2YG09; -.
DR STRING; 426428.A0A0D2YG09; -.
DR EnsemblFungi; FOXG_15247T0; FOXG_15247P0; FOXG_15247.
DR EnsemblFungi; KNB17121; KNB17121; FOXG_15247.
DR GeneID; 28956321; -.
DR KEGG; fox:FOXG_15247; -.
DR VEuPathDB; FungiDB:FOXG_15247; -.
DR OMA; IIQSQRC; -.
DR Proteomes; UP000009097; Chromosome 5.
DR GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:1901605; P:alpha-amino acid metabolic process; IEA:UniProt.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; 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; IPR001341; Asp_kinase.
DR InterPro; IPR018042; Aspartate_kinase_CS.
DR InterPro; IPR027795; CASTOR_ACT_dom.
DR InterPro; IPR011008; Dimeric_a/b-barrel.
DR InterPro; IPR005545; YCII.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF13840; ACT_7; 1.
DR Pfam; PF03795; YCII; 1.
DR SUPFAM; SSF53633; SSF53633; 1.
DR SUPFAM; SSF54909; SSF54909; 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..542
FT /note="Aspartate kinase FUB3"
FT /id="PRO_0000437314"
FT DOMAIN 404..472
FT /note="ACT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT DOMAIN 478..542
FT /note="ACT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
SQ SEQUENCE 542 AA; 59732 MW; 2E83143001B61954 CRC64;
MATELKEYLV IIPDLPDVLA KRQVLLKPHN QDAAPLVKAG RVPFFGSTLA HHSPEGQQVA
ENGTVMIIKA ESEEEIREII RKDIFTIEGV WDFGKLSIWP FKIARMRNRR DNSWVVQKFG
GTSIGKFPDK TSSDMLCTKF RKESLRNNEQ ITADCQELLD YTSAAKRFNL DINGKAKDKM
VSFGEKLSCR LMVAMLRDRD IPAEYVDLSD IVPSNNLDQL KPEFFHEAAA VFGKRVEACN
GRVPVITGFF GTVPGSLIDS GIGRGYSDLC AVLVAIGLHA ERVQIWKEVD GIFTADPREV
PDARCLPSIT PSEAAELTFY GSEVIHHLAL SLAIQAKPPV SIFVKNVQKP WGQGTVVVPS
DGDDTSSWPI DYLDPSDSDS TSSTALPKMP TAVTIKRDIT IFNILSNKQS MSHGFFVKVF
TILAEHDISV DLISTSEVHV SMAINSSNME PSQIKNVQCR LSEEGEVNVL PDMAILSLVG
AELKNMTGIA GRMFAILGEQ HVNIEMISQG ASEINISCVI PDKDATRALN MLHDELFTKS
AI
