FUB5_GIBF5
ID FUB5_GIBF5 Reviewed; 427 AA.
AC S0DUX2;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 25-MAY-2022, entry version 33.
DE RecName: Full=Homoserine O-acetyltransferase FUB5 {ECO:0000303|PubMed:24389666};
DE EC=2.3.1.31 {ECO:0000305|PubMed:26662839};
DE AltName: Full=Fusaric acid biosynthesis protein 5 {ECO:0000303|PubMed:24389666};
GN Name=FUB5 {ECO:0000303|PubMed:24389666}; ORFNames=FFUJ_02109;
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 INDUCTION.
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: 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:24389666, PubMed:26662839). 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 (PubMed:26662839). The polyketide synthase (PKS)
CC FUB1 generates the triketide trans-2-hexenal which is presumptively
CC released by the hydrolase FUB4 and linked to the NRPS-bound amino acid
CC precursor by NAD(P)-dependent dehydrogenase FUB6 (PubMed:26662839).
CC FUB1, FUB4, 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=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:26662839};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:26662839}.
CC -!- INDUCTION: Expressed under high amounts of nitrogen via regulation by
CC AREB (PubMed:24389666). Moreover, components of the fungal-specific
CC velvet complex VEL1 and LAE1 act also as positive regulators of
CC expression (PubMed:24389666). Finally, the pH regulator PACC acts as
CC activator of FUB expression after the pH shift to alkaline ambient
CC conditions (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 AB hydrolase superfamily. MetX family.
CC {ECO:0000305}.
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DR EMBL; HF679025; CCT65187.1; -; Genomic_DNA.
DR AlphaFoldDB; S0DUX2; -.
DR SMR; S0DUX2; -.
DR STRING; 1279085.S0DUX2; -.
DR EnsemblFungi; CCT65187; CCT65187; FFUJ_02109.
DR VEuPathDB; FungiDB:FFUJ_02109; -.
DR HOGENOM; CLU_028760_5_0_1; -.
DR Proteomes; UP000016800; 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..427
FT /note="Homoserine O-acetyltransferase FUB5"
FT /id="PRO_0000437318"
FT DOMAIN 77..400
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 175
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT ACT_SITE 367
FT /evidence="ECO:0000255"
FT ACT_SITE 396
FT /evidence="ECO:0000255"
SQ SEQUENCE 427 AA; 47013 MW; 8E2A747E7D405A4F CRC64;
MTTTTTAPAL PTPIHDGLGN GTTYERSIPR PVNPFSNRVP GREIITVPNF TLESGVEMRN
VPVAYMSWGK LSPKANNVMI ICHALSGSAD VSDWWGPLLG PGKAFDTDKF FVICMNSLGS
PYGTASPVTA KNGDYSEGWY GADFPATTIR DDVRLHKLVL DRLGVRKVAA VIGGSMGGMH
VLEWAFFGKD YVRCIVPAAT SSHQSAWAIG WGEAQRHAIR SDVKYKNGRY GFDDPPILGL
EAARMTALLT YRSRDSLERR FGRDTGNKKK AKNKGSETLP SNSTPIHSQG GADETPVAFD
RADSNFAAQS YLRYQAKKFS DRFDSNCYIA LTNKLDTHDL ARGRTRTITE ALSLIEQPTL
VLGIRSDGLY TLAEQEQIAR TVPNAKLREI VSDDGHDAFL IEWSQLNWLL VGFLHESLPD
IMQRAAL
