FGM3_GIBZE
ID FGM3_GIBZE Reviewed; 402 AA.
AC A0A1C3YKE0; I1S2J7;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=Aminotransferase-like protein FGM3 {ECO:0000303|PubMed:30804501};
DE EC=2.-.-.- {ECO:0000305|PubMed:30804501};
DE AltName: Full=C64 cluster protein NRPS5 {ECO:0000303|PubMed:25333987};
DE AltName: Full=Fg3_54 cluster protein FGM3 {ECO:0000303|PubMed:30804501};
DE AltName: Full=Fusaoctaxin A biosynthesis cluster protein FGM3 {ECO:0000303|PubMed:30804501};
GN Name=FGM3 {ECO:0000303|PubMed:30804501}; ORFNames=FGRAMPH1_01T20965;
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.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RG EnsemblFungi;
RL Submitted (JAN-2017) to UniProtKB.
RN [5]
RP INDUCTION.
RX PubMed=23266949; DOI=10.1105/tpc.112.105957;
RA Zhang X.W., Jia L.J., Zhang Y., Jiang G., Li X., Zhang D., Tang W.H.;
RT "In planta stage-specific fungal gene profiling elucidates the molecular
RT strategies of Fusarium graminearum growing inside wheat coleoptiles.";
RL Plant Cell 24:5159-5176(2012).
RN [6]
RP IDENTIFICATION, AND INDUCTION.
RX PubMed=25333987; DOI=10.1371/journal.pone.0110311;
RA Sieber C.M., Lee W., Wong P., Muensterkoetter M., Mewes H.W., Schmeitzl C.,
RA Varga E., Berthiller F., Adam G., Gueldener U.;
RT "The Fusarium graminearum genome reveals more secondary metabolite gene
RT clusters and hints of horizontal gene transfer.";
RL PLoS ONE 9:e110311-e110311(2014).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30804501; DOI=10.1038/s41467-019-08726-9;
RA Jia L.J., Tang H.Y., Wang W.Q., Yuan T.L., Wei W.Q., Pang B., Gong X.M.,
RA Wang S.F., Li Y.J., Zhang D., Liu W., Tang W.H.;
RT "A linear nonribosomal octapeptide from Fusarium graminearum facilitates
RT cell-to-cell invasion of wheat.";
RL Nat. Commun. 10:922-922(2019).
RN [8]
RP FUNCTION, AND INDUCTION.
RX PubMed=31100892; DOI=10.3390/toxins11050277;
RA Westphal K.R., Nielsen K.A.H., Wollenberg R.D., Moellehoej M.B.,
RA Bachleitner S., Studt L., Lysoee E., Giese H., Wimmer R., Soerensen J.L.,
RA Sondergaard T.E.;
RT "Fusaoctaxin A, an example of a two-step mechanism for non-ribosomal
RT peptide assembly and maturation in fungi.";
RL Toxins 11:0-0(2019).
CC -!- FUNCTION: Aminotransferase-like protein; part of the Fg3_54/C64 gene
CC cluster that mediates the biosynthesis of the octapeptide fusaoctaxin
CC A, a virulence factor that is required for cell-to-cell invasiveness of
CC plant host (PubMed:30804501). The 2 nonribosomal peptide synthetases
CC NRPS9 and NRPS5 form an assembly line which likely utilizes GABA as a
CC starter unit (loaded on the unique module M1 of NRPS9) and sequentially
CC incorporates seven extender units composed of the residues L-Ala, L-
CC allo-Ile, L-Ser, L-Val, L-Ser, L-Leu and L-Leu, respectively
CC (PubMed:30804501, PubMed:31100892). During the process, each of the
CC residues that are tethered on modules M3-M7 of NRPS5 containing an E
CC domain can undergo an epimerization reaction to produce a D-
CC configuration before the transpeptidation reaction occurs
CC (PubMed:30804501, PubMed:31100892). The elongation of the peptidyl
CC chain might be terminated by module M8-mediated L-Leu incorporation,
CC followed by R domain-catalyzed 4 electron reduction to release the
CC resulting octapeptide from the assembly line as an alcohol
CC (PubMed:30804501, PubMed:31100892). Fusaoctaxin A is cleaved by the
CC cluster specific ABC transporter FGM5 to the pentapeptide fusapentaxin
CC A and the tripeptide fusatrixin A (PubMed:31100892). The other enzymes
CC from the cluster, FGM1, FGM2, FGM3 and FGM9 seem not to be involved in
CC the biosynthesis of fusaoctaxin A and their functions have still to be
CC determined (Probable). {ECO:0000269|PubMed:30804501,
CC ECO:0000269|PubMed:31100892, ECO:0000305|PubMed:30804501}.
CC -!- INDUCTION: Expression is positively regulated by the cluster-specific
CC transcription factor FGM4 and is induced during infection of
CC coleoptiles of wheat seedlings (PubMed:23266949, PubMed:25333987). The
CC fusaoctaxin A gene cluster is silenced by H3K27 trimethylation by the
CC histone methyltransferase KMT6 (PubMed:31100892).
CC {ECO:0000269|PubMed:23266949, ECO:0000269|PubMed:25333987,
CC ECO:0000269|PubMed:31100892}.
CC -!- DISRUPTION PHENOTYPE: Produces fewer spikelets with blight symptoms on
CC susceptible wheat cultivars. {ECO:0000269|PubMed:30804501}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. Csd subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=SCB64986.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; HG970334; SCB64986.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; A0A1C3YKE0; -.
DR SMR; A0A1C3YKE0; -.
DR STRING; 5518.FGSG_10993P0; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G20965; -.
DR eggNOG; KOG1549; Eukaryota.
DR HOGENOM; CLU_003433_2_2_1; -.
DR PHI-base; PHI:9038; -.
DR Proteomes; UP000070720; Chromosome 3.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00266; Aminotran_5; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 2: Evidence at transcript level;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..402
FT /note="Aminotransferase-like protein FGM3"
FT /id="PRO_0000449948"
FT BINDING 137..138
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q96255"
FT BINDING 218
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q96255"
FT BINDING 282..283
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q96255"
SQ SEQUENCE 402 AA; 43942 MW; ED97C11777F52F47 CRC64;
MSSSSFSIEN VRSQFPALEK RQIFGDNAGG SQVLGTVAKR QLSPITEYLI ETNVQLGASY
KTSTQSTAIF DNAYKAAAKY INAGIDEIVI GASTTQVFRN LAAALKLQPG DELILTNVDH
ESNIDPWLHY AALNNATIKW WTPSDLNNPK LDPEQLRSLL TNKTRLVACT HCSNILGTIN
NIKAIADVVH EIPGALLAVD GVAYAPHRAI DVKELGADFY AFSWYKVYGP HISLLYGSKA
AQAQLSSLGH FFNPDGSLMD KLELAAASYE LTQAIIPLTA YFGENPKQTW DAIAEHEQKL
QTRLIEYLVS KPQITVYGET STDKAVRVPT VSFTVEGMSS QSVVEAVEAV SHAGIRWGHF
FSKRLVGSIL GLSDDGVVRV SLVHYNTVEE VDQIIVALEM VL
