FUB5_GIBM7
ID FUB5_GIBM7 Reviewed; 463 AA.
AC W7N293;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=Homoserine O-acetyltransferase FUB5 {ECO:0000303|PubMed:22652150};
DE EC=2.3.1.31 {ECO:0000305|PubMed:25372119};
DE AltName: Full=Fusaric acid biosynthesis protein 5 {ECO:0000303|PubMed:22652150};
GN Name=FUB5 {ECO:0000303|PubMed:22652150}; ORFNames=FVEG_12519;
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.
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: Homoserine O-acetyltransferase; part of the gene cluster that
CC mediates the biosynthesis of fusaric acid, a mycotoxin with low to
CC moderate toxicity to animals and humans, but with high phytotoxic
CC properties (PubMed:22652150, PubMed:25372119). L-aspartate is suggested
CC as fusaric acid amino acid precursor that is activated and further
CC processed to O-acetyl-L-homoserine by cluster enzymes aspartate kinase
CC FUB3 and homoserine O-acetyltransferase FUB5, as well as enzymes of the
CC primary 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:S0DUX2,
CC ECO:0000269|PubMed:22652150, ECO:0000269|PubMed:25372119}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine;
CC Xref=Rhea:RHEA:13701, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57476, ChEBI:CHEBI:57716; EC=2.3.1.31;
CC Evidence={ECO:0000305|PubMed:25372119};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:22652150,
CC ECO:0000269|PubMed:25372119}.
CC -!- INDUCTION: Expression is positively regulated by the secondary
CC metabolism regulator LAE1 (PubMed:22713715).
CC {ECO:0000269|PubMed:22713715}.
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 AB hydrolase superfamily. MetX family.
CC {ECO:0000305}.
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DR EMBL; DS022261; EWG54260.1; -; Genomic_DNA.
DR RefSeq; XP_018760451.1; XM_018901859.1.
DR AlphaFoldDB; W7N293; -.
DR SMR; W7N293; -.
DR STRING; 117187.FVEG_12519T0; -.
DR EnsemblFungi; FVEG_12519T0; FVEG_12519T0; FVEG_12519.
DR GeneID; 30069953; -.
DR KEGG; fvr:FVEG_12519; -.
DR VEuPathDB; FungiDB:FVEG_12519; -.
DR eggNOG; ENOG502QRIX; Eukaryota.
DR HOGENOM; CLU_028760_5_0_1; -.
DR OMA; WDQARSI; -.
DR OrthoDB; 1090515at2759; -.
DR PHI-base; PHI:3391; -.
DR Proteomes; UP000009096; Chromosome 3.
DR GO; GO:0004414; F:homoserine O-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.1820; -; 1.
DR HAMAP; MF_00296; MetX_acyltransf; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR008220; HAT_MetX-like.
DR PANTHER; PTHR32268; PTHR32268; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF000443; Homoser_Ac_trans; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR01392; homoserO_Ac_trn; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Transferase.
FT CHAIN 1..463
FT /note="Homoserine O-acetyltransferase FUB5"
FT /id="PRO_0000437319"
FT DOMAIN 113..436
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT REGION 296..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 211
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT ACT_SITE 403
FT /evidence="ECO:0000255"
FT ACT_SITE 432
FT /evidence="ECO:0000255"
SQ SEQUENCE 463 AA; 51037 MW; B987C58088A298D6 CRC64;
MSRRQTLKTL QKLILAPSQH ISLSIASNLS VIPSRSMTTT ATVPVLPTSI HDGLGKGIAY
EKSLPRPVNP FSHRVPGREI ITIPKFTLES GVEMRNVPVA YMSWGKLSSK ANNVMIICHA
LSGSADVSDW WGPLLGHGKA FDTDKFFVIC MNSLGSPYGT ASPVTAKNGD YSEGWYGADF
PSTTIRDDVR LHKLALDKLG VRKVAAAIGG SMGGMHVLEW AFFGKDYVRC IVPAATSSHQ
SAWAIGWGEA QRHAIRSDVK YKNGRYGFDD PPVLGLEAAR MTALLTYRSR DSLERRFGRD
TGSKKKTQKQ ESKTLPSNST PIHSHSGADE TPVAFDRADS SFAAQSYLRY QAKKFSNRFD
SNCYIALTNK LDTHDLARGR TRTITEALSL IEQPTLVLGI RSDGLYTLAE QEQIARAVPN
AKLREIVSDD GHDAFLIEWS QLNWLLIGFL HESLPDIMQR AAL
