ID FUSA3_GIBZE Reviewed; 511 AA.
AC A0A098DDI1; A0A0E0RZ10;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Aminotransferase FGSG_17085 {ECO:0000303|PubMed:25412204};
DE EC=2.6.-.- {ECO:0000305|PubMed:25412204};
DE AltName: Full=Fusaristatin A biosynthesis cluster protein FGSG_17085 {ECO:0000303|PubMed:25412204};
GN ORFNames=FGRAMPH1_01T09365, FGSG_0820,
GN FGSG_17085 {ECO:0000303|PubMed:25412204};
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 IDENTIFICATION, FUNCTION, AND PATHWAY.
RX PubMed=25412204; DOI=10.1021/np500436r;
RA Soerensen J.L., Sondergaard T.E., Covarelli L., Fuertes P.R., Hansen F.T.,
RA Frandsen R.J., Saei W., Lukassen M.B., Wimmer R., Nielsen K.F.,
RA Gardiner D.M., Giese H.;
RT "Identification of the biosynthetic gene clusters for the lipopeptides
RT fusaristatin A and W493 B in Fusarium graminearum and F.
RT pseudograminearum.";
RL J. Nat. Prod. 77:2619-2625(2014).
CC -!- FUNCTION: Aminotransferase; part of the gene cluster that mediates the
CC biosynthesis of the lipopeptide fusaristatin A (PubMed:25412204).
CC Fusaristatin A consists of a polyketide chain linked to three amino
CC acid residues glutamine (Gln), dehydroalanine (dehydro-Ala), and beta-
CC aminoisobutyric acid (PubMed:25412204). The biosynthesis starts with
CC formation of a linear polyketide chain by the highly reducing
CC polyketide synthase PKS6 (PubMed:25412204). The gene cluster does not
CC contain an acyl-CoA ligase or an acyl-transferase, and it is therefore
CC predicted that the polyketide is transferred directly to the
CC nonribosomal peptide synthetase NRPS7 (Probable). Modules 1-3 from
CC NRPS7 incorporate dehydro-Ala, Gln, and beta-aminoisobutyric acid in
CC the compound, which is released by cyclization (PubMed:25412204). The
CC beta-aminoisobutyric acid units are most likely not freely available to
CC the NRPS, but can be synthesized from thymine, which requires a
CC dehydrogenase, a monooxygenase, and an aminotransferase. The
CC fusaristatin A cluster contains a cytochrome P450 monooxygenase
CC (FGSG_08207) and an aminotransferase (FGSG_17085), which theoretically
CC can perform two of the enzymatic steps (Probable). The enzymes may
CC however also be involved in biosynthesis of dehydroalanine or
CC modification of the polyketide (Probable). The dehydro-Ala residue can
CC be a result of cyclization, where serine is dehydrated (Probable). The
CC last gene of the cluster encodes a protein with an A/B barrel domain
CC found in variable enzymes, which hampers functional prediction
CC (Probable). {ECO:0000269|PubMed:25412204, ECO:0000305|PubMed:25412204}.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P53555};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:25412204}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; HG970333; CEF76485.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A098DDI1; -.
DR SMR; A0A098DDI1; -.
DR STRING; 229533.A0A098DDI1; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G09365; -.
DR InParanoid; A0A098DDI1; -.
DR Proteomes; UP000070720; Chromosome 2.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43094; AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..511
FT /note="Aminotransferase FGSG_17085"
FT /id="PRO_0000445376"
FT BINDING 165..166
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P53555"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53555"
FT BINDING 310
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12995"
FT BINDING 371
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53555"
FT BINDING 372..373
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P53555"
FT MOD_RES 339
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P53555"
SQ SEQUENCE 511 AA; 55628 MW; 6072E99048B6F30C CRC64;
MFATQSPRHL QVLLCRTKKF ALASPPICYK VGAASSGSIR KFLSARFSTS ARARNLKQSV
LDNSGRHGVY LYPTLKPEPL NVVSAKDTTV VFSNGKTIED TTCGAAVACL GYNNERVKNA
MIKQMDSFCY SNSLFYGHEI GEELAAELIG GTNGEMAKVY LMCSGAEAME SAMKMARQYY
MELNPRQPQR TNFIAREGSY HGSTLGALSM GGHVGRRKLF EGMLLDNNIH RVSAANEYRG
KADGQTTEEY VQQLADELDR KFQEVGPETV AAFVAETLVG ATLGTIPAPT GYFKAMKKVC
DKYGALLILD EVMCGMGRCG SLHEWEQEGV VPDIQTVAKG LAGGFAPMAA MFINHRLSDA
LMSGSGVFSH GHTYQGHPVG CAAALEVQRI IREDNLVENV RKNGEYLGKL LHDQLDDHPN
VGNIRGRGFF WSMEFVADKE TKEPFLPSDG IAKKVHLTAL NDVGISLYPG MGTKDGVAGD
HAWIGPAYNC SKQDIERIVS KVKEAVVLAL G
//
