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FUB5_FUSO4
ID   FUB5_FUSO4              Reviewed;         362 AA.
AC   A0A0D2YG05;
DT   05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2015, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Homoserine O-acetyltransferase FUB5 {ECO:0000303|PubMed:25372119};
DE            EC=2.3.1.31 {ECO:0000305|PubMed:25372119};
DE   AltName: Full=Fusaric acid biosynthesis protein 5 {ECO:0000303|PubMed:25372119};
GN   Name=FUB5 {ECO:0000303|PubMed:25372119}; ORFNames=FOXG_15243;
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, 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: 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:25372119). L-aspartate is suggested as fusaric acid
CC       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 O-acetylhomoserine 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: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: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 AB hydrolase superfamily. MetX family.
CC       {ECO:0000305}.
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DR   EMBL; DS231721; KNB17117.1; -; Genomic_DNA.
DR   EMBL; DS231721; KNB17118.1; -; Genomic_DNA.
DR   RefSeq; XP_018255162.1; XM_018395328.1.
DR   RefSeq; XP_018255163.1; XM_018395329.1.
DR   AlphaFoldDB; A0A0D2YG05; -.
DR   SMR; A0A0D2YG05; -.
DR   STRING; 426428.A0A0D2YG05; -.
DR   EnsemblFungi; FOXG_15243T0; FOXG_15243P0; FOXG_15243.
DR   EnsemblFungi; KNB17117; KNB17117; FOXG_15243.
DR   EnsemblFungi; KNB17118; KNB17118; FOXG_15243.
DR   GeneID; 28956319; -.
DR   KEGG; fox:FOXG_15243; -.
DR   VEuPathDB; FungiDB:FOXG_15243; -.
DR   OMA; WDQARSI; -.
DR   Proteomes; UP000009097; Chromosome 5.
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..362
FT                   /note="Homoserine O-acetyltransferase FUB5"
FT                   /id="PRO_0000437320"
FT   DOMAIN          12..335
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   REGION          195..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..224
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        110
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        302
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        331
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   362 AA;  40029 MW;  F4F152F0F20099E9 CRC64;
     MSWGKLSPKA NNVMIICHAL SGSADVSDWW GPLLGPGKAF DTDKFFVVCM NSLGSPYGTA
     SPVTAKNGDY SQGWYGADFP STTIRDDVRL HKLVLDKLGV RKVAAVIGGS MGGMHVLEWA
     FFGKDYVRCI VPAATSSHQS AWAIGWGEAQ RHAIRSDVKY KNGRYGFDDP PILGLEAARM
     TALLTYRSRD SLERRFGRDT GNKKKTQQQD SKTIPNNGTP IHSQGGADET PVAFDRADSN
     FAAQSYLRYQ AKKFSDRFDS NCYIALTNKL DTHDLARGRT RTIAEALSLI QQPTLVLGIR
     SDGLYTLAEQ EQIARAVPNA KLREIVSDDG HDAFLIEWSQ LNWLLIGFLH ENLPDIMQRA
     AL
 
 
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