GRA10_GIBZE
ID GRA10_GIBZE Reviewed; 344 AA.
AC I1R9B0; A0A098D0A5;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Thioredoxin reductase FGSG_00043 {ECO:0000303|PubMed:30395461};
DE EC=1.8.1.- {ECO:0000305|PubMed:30395461};
DE AltName: Full=Gramillins biosynthetic cluster protein FGSG_00043 {ECO:0000303|PubMed:30395461};
GN ORFNames=FG00043, FGRAMPH1_01T00145, FGSG_00043;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4]
RP FUNCTION, AND PATHWAY.
RX PubMed=30395461; DOI=10.1021/jacs.8b10017;
RA Bahadoor A., Brauer E.K., Bosnich W., Schneiderman D., Johnston A.,
RA Aubin Y., Blackwell B., Melanson J.E., Harris L.J.;
RT "Gramillin A and B: cyclic lipopeptides identified as the nonribosomal
RT biosynthetic products of Fusarium graminearum.";
RL J. Am. Chem. Soc. 140:16783-16791(2018).
CC -!- FUNCTION: Thioredoxin reductase; part of the gene cluster that mediates
CC the biosynthesis of gramillins A and B, bicyclic lipopeptides that
CC induce cell death in maize leaves but not in wheat leaves
CC (PubMed:30395461). The nonribosomal peptide synthetase GRA1
CC incorporates respectively a glutamic adic (Glu), a leucine (Leu), a
CC serine (Ser), a hydroxyglutamine (HOGln), a 2-amino decanoic acid, and
CC 2 cysteins (CysB and CysA) (Probable). The biosynthesis of 2-amino
CC decanoic acid incorporated in gramillins could be initiated by a fatty
CC acid synthase composed of the alpha and beta subunits FGSG_00036 and
CC FGSG_11656 (Probable). The cytochrome P450 monooxygenase FGSG_15680
CC could hydroxylate the fatty acid chain (Probable). Subsequent oxidation
CC to the ketone by the oxidoreductase FGSG_00048 and transamination by
CC aminotransferase FGSG_00049 could form 2-amino-decanoic acid
CC (Probable). On the other hand, FGSG_15680 could also be responsible for
CC the HO-modified glutamine at the gamma-position (Probable). Whether
CC hydroxylation occurs on the fully assembled product or on the Gln
CC residue prior to assembly into the gramillins requires further proof
CC (Probable). The thioredoxin FGSG_00043 could also be required for the
CC disulfide-bond formation between CysA and CysB (Probable). The specific
CC involvement of the remaining proteins from the cluster is more
CC difficult to discern, but could have broader regulatory (FGSG_00040 and
CC FGSG_11657) or enzymatic functions (FGSG_00044 and FGSG_00045)
CC (Probable). The final C-domain of GRA1 does not possess the expected
CC sequence of a termination CT domain, often implicated in
CC macrocyclization and release of a cyclopeptidein fungal NRPs; and the
CC thioesterase FGSG_00047 may act in concert with the terminal C-domain
CC of GRA1 to catalyze the formation of the macrocyclic anhydride and
CC release of the products (Probable). {ECO:0000269|PubMed:30395461,
CC ECO:0000305|PubMed:30395461}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:E9RAH5};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:E9RAH5};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:30395461}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:E9RAH5}.
CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; HG970332; CEF71872.1; -; Genomic_DNA.
DR RefSeq; XP_011315632.1; XM_011317330.1.
DR AlphaFoldDB; I1R9B0; -.
DR SMR; I1R9B0; -.
DR STRING; 5518.FGSG_00043P0; -.
DR GeneID; 23547559; -.
DR KEGG; fgr:FGSG_00043; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G00145; -.
DR eggNOG; ENOG502S1DJ; Eukaryota.
DR HOGENOM; CLU_031864_5_0_1; -.
DR InParanoid; I1R9B0; -.
DR Proteomes; UP000070720; Chromosome 1.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 3: Inferred from homology;
KW Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW Redox-active center; Reference proteome; Virulence.
FT CHAIN 1..344
FT /note="Thioredoxin reductase FGSG_00043"
FT /id="PRO_0000450565"
FT BINDING 12..15
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9RAH5"
FT BINDING 34..39
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9RAH5"
FT BINDING 51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9RAH5"
FT BINDING 121
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9RAH5"
FT BINDING 314
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9RAH5"
FT BINDING 321..322
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E9RAH5"
FT DISULFID 165..168
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:E9RAH5"
SQ SEQUENCE 344 AA; 37460 MW; 6C36CCD0251BD973 CRC64;
MSQIIDALVI GGGPAGLGAA LGLCRQNHSV VLLDSVSYRN TIDTIPDNRM HMVATWDHRR
PDEFRVAARK ELQRYERFKY REVEVVSVRQ TTSTQSGKLE ALFNAKAADG TEYAARKLIL
ATGVKDVFPK IEGFSECWAK GMYVLSPNSN ELCIARETKY RSFHCLFCHG YEDRNSESVG
VLAVGECAET STVARMARAA HQFSRSITIY TNGNSELGDQ VYRLLGKEGW CSINNLGIKK
VYMPQKTPAS PITVQVELSD GTTKTEDFLV HKPATVQASA LYTQLGLQLT AEGDIKVKEP
MFETSKAGVF AVGDCASPNK FVSSASTSGG FAAAGAAMQL QAGF
