FUB3_GIBF5
ID FUB3_GIBF5 Reviewed; 510 AA.
AC S0DVT6;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Aspartate kinase FUB3 {ECO:0000303|PubMed:24389666};
DE EC=2.7.2.4 {ECO:0000305|PubMed:26662839};
DE AltName: Full=Fusaric acid biosynthesis protein 3 {ECO:0000303|PubMed:24389666};
GN Name=FUB3 {ECO:0000303|PubMed:24389666}; ORFNames=FFUJ_02107;
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 DISRUPTION PHENOTYPE.
RX PubMed=24389666; DOI=10.1007/s00253-013-5453-1;
RA Niehaus E.M., von Bargen K.W., Espino J.J., Pfannmueller A., Humpf H.U.,
RA Tudzynski B.;
RT "Characterization of the fusaric acid gene cluster in Fusarium fujikuroi.";
RL Appl. Microbiol. Biotechnol. 98:1749-1762(2014).
RN [10]
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: 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:24389666, PubMed:26662839). 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 (PubMed:26662839). 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 (PubMed:26662839). FUB1, FUB4,
CC and 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:24389666, ECO:0000269|PubMed:26662839}.
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:26662839};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:26662839}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of fusaric acid
CC (PubMed:24389666). {ECO:0000269|PubMed:24389666}.
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; HF679025; CCT66674.1; -; Genomic_DNA.
DR AlphaFoldDB; S0DVT6; -.
DR SMR; S0DVT6; -.
DR STRING; 1279085.S0DVT6; -.
DR PRIDE; S0DVT6; -.
DR EnsemblFungi; CCT66674; CCT66674; FFUJ_02107.
DR VEuPathDB; FungiDB:FFUJ_02107; -.
DR HOGENOM; CLU_009116_6_4_1; -.
DR Proteomes; UP000016800; 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; 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.
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_0000437312"
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; 55994 MW; 339BBE6F9A3A88E0 CRC64;
MRSRRDNSWV AQKFGGTSIG KFPDKVAEIV KSARLGGDRP AVICSARSSG KKVFGTTSRL
LQVYRTLRGI VAITQDPDMQ ELLFDRLRSI IRDIRDDQVA TVQMYILRQD IRDDTIRQIT
ADCQELLDYT SAAKRFNLDI NGKAKDKMVS FGEKLSCRLM VAMLRDRDIP AEYVDLSDIV
PSNNLDQLRP DFFHEAAAVF GKRVEACNGR VPVITGFFGA VPGSLIDSGI GRGYSDLCAV
LVAIGLHAER VQIWKEVDGI FTADPREVPD ARCLPSITPS EAAELTFYGS EVIHHLALSL
AIQAKPPVSI FVKNVQKPWG QGTVVVPTDG DDTSSWPIDY LDPSDSDSTS STALPKMPTA
VTIKRDITIF NILSNKQSMS HGFFVKVFTI LAEHDISVDL ISTSEVHVSM AINSSNMDPS
QIKNVQCRLA EEGEVNVLPD MAILSLVGAE LKNMTGIAGK MFAILGEQDV NIEMISQGAS
EINISCVIPD KDATRALNML HDELFTKNAI
