FGM2_GIBZE
ID FGM2_GIBZE Reviewed; 338 AA.
AC I1S2J6; A0A098E518;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Peptidoglycan deacetylase-like protein FGM2 {ECO:0000303|PubMed:30804501};
DE EC=3.5.-.- {ECO:0000305|PubMed:30804501};
DE AltName: Full=C64 cluster protein NRPS5 {ECO:0000303|PubMed:25333987};
DE AltName: Full=Fg3_54 cluster protein FGM2 {ECO:0000303|PubMed:30804501};
DE AltName: Full=Fusaoctaxin A biosynthesis cluster protein FGM2 {ECO:0000303|PubMed:30804501};
GN Name=FGM2 {ECO:0000303|PubMed:30804501};
GN ORFNames=FG10992, FGRAMPH1_01T20963;
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, AND DISRUPTION PHENOTYPE.
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: Peptidoglycan deacetylase-like protein; part of the
CC Fg3_54/C64 gene cluster that mediates the biosynthesis of the
CC octapeptide fusaoctaxin A, a virulence factor that is required for
CC cell-to-cell invasiveness of plant host (PubMed:30804501). The 2
CC nonribosomal peptide synthetases NRPS9 and NRPS5 form an assembly line
CC which likely utilizes GABA as a starter unit (loaded on the unique
CC module M1 of NRPS9) and sequentially incorporates seven extender units
CC composed of the residues L-Ala, L-allo-Ile, L-Ser, L-Val, L-Ser, L-Leu
CC and L-Leu, respectively (PubMed:30804501, PubMed:31100892). During the
CC process, each of the residues that are tethered on modules M3-M7 of
CC NRPS5 containing an E domain can undergo an epimerization reaction to
CC produce a D-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: Leads to reduced virulence and produces
CC significantly smaller lesions and fewer spikelets with blight symptoms
CC on susceptible wheat cultivars. {ECO:0000269|PubMed:23266949,
CC ECO:0000269|PubMed:30804501}.
CC -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC {ECO:0000305}.
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DR EMBL; HG970334; CEF88824.1; -; Genomic_DNA.
DR RefSeq; XP_011325378.1; XM_011327076.1.
DR AlphaFoldDB; I1S2J6; -.
DR SMR; I1S2J6; -.
DR STRING; 5518.FGSG_10992P0; -.
DR GeneID; 23557866; -.
DR KEGG; fgr:FGSG_10992; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G20963; -.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_029940_1_0_1; -.
DR InParanoid; I1S2J6; -.
DR PHI-base; PHI:9039; -.
DR Proteomes; UP000070720; Chromosome 3.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd10938; CE4_HpPgdA_like; 1.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR InterPro; IPR037950; PgdA-like.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
DR PROSITE; PS51677; NODB; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..338
FT /note="Peptidoglycan deacetylase-like protein FGM2"
FT /id="PRO_0000449949"
FT DOMAIN 65..257
FT /note="NodB homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:B5ZA76"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:B5ZA76"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:B5ZA76"
SQ SEQUENCE 338 AA; 37828 MW; 1CE9D6EF5AC5A0D4 CRC64;
MQIDHSGDSS EASQAHDSKL HHSHLLGNIP LGLPEARRRV KILVSVDFDA VSGWMGTGQH
SRNCLSDYSA GIFAGRVGVG RLLKILDRVG IAEKVTWFIP GHSMETFPLE TKAIVDSGAE
IALHGYCHED CTQLDPQQQQ DILDKCITLA ESLTGKRPVG FRAPLYRIDH DTISLLERKG
FLYDTSLSGH DAQLYYLDSG FPLDVVDYSK SASTWMKPSP QPRQLSVVEI PANWYMEDMT
PMQFLPNVTN SHGFVSSEAI EKMWKDRFNW LWNWGPDGSG PGDFVFPLVL HPDTSGMAHV
AGTIEGMLRW LKEWGPQVEF VTYEEAAREF LLDKEVPA
