GRA16_GIBZE
ID GRA16_GIBZE Reviewed; 382 AA.
AC I1R9B6; A0A098CZ47;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Aminotransferase FGSG_00049 {ECO:0000303|PubMed:30395461};
DE EC=2.6.1.- {ECO:0000305|PubMed:30395461};
DE AltName: Full=Gramillins biosynthesis cluster protein FGSG_00049 {ECO:0000303|PubMed:30395461};
GN ORFNames=FGRAMPH1_01T00157, FGSG_00049;
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: Aminotransferase; part of the gene cluster that mediates the
CC biosynthesis of gramillins A and B, bicyclic lipopeptides that induce
CC cell death in maize leaves but not in wheat leaves (PubMed:30395461).
CC The nonribosomal peptide synthetase GRA1 incorporates respectively a
CC glutamic adic (Glu), a leucine (Leu), a serine (Ser), a
CC hydroxyglutamine (HOGln), a 2-amino decanoic acid, and 2 cysteins (CysB
CC and CysA) (Probable). The biosynthesis of 2-amino decanoic acid
CC incorporated in gramillins could be initiated by a fatty acid synthase
CC composed of the alpha and beta subunits FGSG_00036 and FGSG_11656
CC (Probable). The cytochrome P450 monooxygenase FGSG_15680 could
CC hydroxylate the fatty acid chain (Probable). Subsequent oxidation to
CC 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=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P19938};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:30395461}.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; HG970332; CEF71878.1; -; Genomic_DNA.
DR RefSeq; XP_011315638.1; XM_011317336.1.
DR AlphaFoldDB; I1R9B6; -.
DR SMR; I1R9B6; -.
DR STRING; 5518.FGSG_00049P0; -.
DR GeneID; 23547565; -.
DR KEGG; fgr:FGSG_00049; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G00157; -.
DR eggNOG; KOG0975; Eukaryota.
DR HOGENOM; CLU_031922_1_0_1; -.
DR InParanoid; I1R9B6; -.
DR Proteomes; UP000070720; Chromosome 1.
DR GO; GO:0004084; F:branched-chain-amino-acid transaminase activity; IEA:InterPro.
DR GO; GO:0009081; P:branched-chain amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.20.10.10; -; 1.
DR Gene3D; 3.30.470.10; -; 1.
DR InterPro; IPR001544; Aminotrans_IV.
DR InterPro; IPR036038; Aminotransferase-like.
DR InterPro; IPR005786; B_amino_transII.
DR InterPro; IPR043132; BCAT-like_C.
DR InterPro; IPR043131; BCAT-like_N.
DR PANTHER; PTHR42825; PTHR42825; 1.
DR Pfam; PF01063; Aminotran_4; 1.
DR PIRSF; PIRSF006468; BCAT1; 1.
DR SUPFAM; SSF56752; SSF56752; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase;
KW Virulence.
FT CHAIN 1..382
FT /note="Aminotransferase FGSG_00049"
FT /id="PRO_0000450567"
FT BINDING 80
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P19938"
FT BINDING 217
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P19938"
FT MOD_RES 181
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P19938"
SQ SEQUENCE 382 AA; 41801 MW; 8C24DA1F583DE2CD CRC64;
MVKILPPTAS IDWDQISIAT NLGLGHVEST YHMSTGRWSD PVFVNDPYLR VHGLAPGLQY
AFRTPKGRVS IFRPDKHAKR MSHSTSTISI PNIPESLFLA SVELAVTSNS SYVPPHTSRA
MLYIRPFAFG SSEMIGLVPP SEYKFCVYVK PVPAYHGLSA QDALILTGFD RAAPHGLGHA
KVGGNYAPVI KWSEQAKADG FGMTLHLDSK TRTEIDEFST SGFLGIKVSD EGAVKVVAPS
SPCIIDSTTS DCCLQLARHY GWNVEKRPIK YTELPEFSEV VAVGTAASVV SIRSITLEDS
RETVRYLDAT TNQGRYARKL STSLDDIMHC RVEDVFGWCH QVGEAPVEDV PTRKMGSSNK
KPAFVDIMTL SCAGQGARFS CH
