FUB7_FUSO4
ID FUB7_FUSO4 Reviewed; 433 AA.
AC A0A0D2YG02;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=Sulfhydrylase FUB7 {ECO:0000303|PubMed:25372119};
DE EC=2.5.1.- {ECO:0000305|PubMed:25372119};
DE AltName: Full=Fusaric acid biosynthesis protein 7 {ECO:0000303|PubMed:25372119};
GN Name=FUB7 {ECO:0000303|PubMed:25372119}; ORFNames=FOXG_15240;
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: Sulfhydrylase; 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:S0DUX5,
CC ECO:0000269|PubMed:25372119}.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P50125};
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 trans-sulfuration enzymes family.
CC {ECO:0000305}.
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DR EMBL; DS231721; KNB17098.1; -; Genomic_DNA.
DR EMBL; DS231721; KNB17099.1; -; Genomic_DNA.
DR EMBL; DS231721; KNB17100.1; -; Genomic_DNA.
DR EMBL; DS231721; KNB17101.1; -; Genomic_DNA.
DR EMBL; DS231721; KNB17102.1; -; Genomic_DNA.
DR EMBL; DS231721; KNB17103.1; -; Genomic_DNA.
DR EMBL; DS231721; KNB17104.1; -; Genomic_DNA.
DR EMBL; DS231721; KNB17105.1; -; Genomic_DNA.
DR EMBL; DS231721; KNB17106.1; -; Genomic_DNA.
DR EMBL; DS231721; KNB17107.1; -; Genomic_DNA.
DR EMBL; DS231721; KNB17108.1; -; Genomic_DNA.
DR EMBL; DS231721; KNB17109.1; -; Genomic_DNA.
DR EMBL; DS231721; KNB17110.1; -; Genomic_DNA.
DR EMBL; DS231721; KNB17111.1; -; Genomic_DNA.
DR EMBL; DS231721; KNB17112.1; -; Genomic_DNA.
DR RefSeq; XP_018255143.1; XM_018395311.1.
DR RefSeq; XP_018255144.1; XM_018395312.1.
DR RefSeq; XP_018255145.1; XM_018395318.1.
DR RefSeq; XP_018255146.1; XM_018395319.1.
DR RefSeq; XP_018255147.1; XM_018395320.1.
DR RefSeq; XP_018255148.1; XM_018395321.1.
DR RefSeq; XP_018255149.1; XM_018395322.1.
DR RefSeq; XP_018255150.1; XM_018395323.1.
DR RefSeq; XP_018255151.1; XM_018395324.1.
DR RefSeq; XP_018255152.1; XM_018395325.1.
DR RefSeq; XP_018255153.1; XM_018395313.1.
DR RefSeq; XP_018255154.1; XM_018395314.1.
DR RefSeq; XP_018255155.1; XM_018395315.1.
DR RefSeq; XP_018255156.1; XM_018395316.1.
DR RefSeq; XP_018255157.1; XM_018395317.1.
DR AlphaFoldDB; A0A0D2YG02; -.
DR SMR; A0A0D2YG02; -.
DR STRING; 426428.A0A0D2YG02; -.
DR EnsemblFungi; FOXG_15240T0; FOXG_15240P0; FOXG_15240.
DR EnsemblFungi; KNB17098; KNB17098; FOXG_15240.
DR EnsemblFungi; KNB17099; KNB17099; FOXG_15240.
DR EnsemblFungi; KNB17100; KNB17100; FOXG_15240.
DR EnsemblFungi; KNB17101; KNB17101; FOXG_15240.
DR EnsemblFungi; KNB17102; KNB17102; FOXG_15240.
DR EnsemblFungi; KNB17103; KNB17103; FOXG_15240.
DR EnsemblFungi; KNB17104; KNB17104; FOXG_15240.
DR EnsemblFungi; KNB17105; KNB17105; FOXG_15240.
DR EnsemblFungi; KNB17106; KNB17106; FOXG_15240.
DR EnsemblFungi; KNB17107; KNB17107; FOXG_15240.
DR EnsemblFungi; KNB17108; KNB17108; FOXG_15240.
DR EnsemblFungi; KNB17109; KNB17109; FOXG_15240.
DR EnsemblFungi; KNB17110; KNB17110; FOXG_15240.
DR EnsemblFungi; KNB17111; KNB17111; FOXG_15240.
DR EnsemblFungi; KNB17112; KNB17112; FOXG_15240.
DR GeneID; 28956316; -.
DR KEGG; fox:FOXG_15240; -.
DR VEuPathDB; FungiDB:FOXG_15240; -.
DR OMA; TTHSQMN; -.
DR Proteomes; UP000009097; Chromosome 5.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR CDD; cd00614; CGS_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR006235; OAc-hSer/O-AcSer_sulfhydrylase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01326; OAH_OAS_sulfhy; 1.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 1: Evidence at protein level;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..433
FT /note="Sulfhydrylase FUB7"
FT /id="PRO_0000437338"
FT MOD_RES 211
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P06721"
SQ SEQUENCE 433 AA; 47110 MW; 6C1F64DEABE346F0 CRC64;
MAEQVFQNFE TLQLHAGYTP DPHTRSTAVP IYATSSYTFN DSAHGARLFG LKELGNIYSR
LMNPTVDVFE KRIAALEGGI AAAATSSGQA AQFLTIATLA KAGDNIVASS HLYGGTYNQL
NVLLPRFGIK TKFVRSGKLE DYAAAIDDQT RAIYVESMSN PDYVVPDFEG IAKIAHEHGI
PLVVDNTLGA GGYYIRPIEH GADIVVHSAT KWIGGHGTTI GGVIVDSGRF NWNKHSERFP
EMVEPSPSYH GLKYWEAFGP ATFITRIRVE MLRDIGACLS PFSAQQLLLG IETLGLRAER
HAQNTEKLAK YFESSPNVSW VLWPGSESHP TYAQAKKYLT RGFGAMLSIG VKGDASAGSK
VVDGLKLVSN LANVGDAKSL AIHPWSTTHE QLSEDERLAS GVTEDMIRIS VGIEHVDDII
ADFEQSFQKA YGS
