NRPS9_GIBZE
ID NRPS9_GIBZE Reviewed; 819 AA.
AC I1S2J4; A0A098E2D6;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Nonribosomal peptide synthetase 9 {ECO:0000303|PubMed:30804501};
DE Short=NRPS 9 {ECO:0000303|PubMed:30804501};
DE EC=6.3.2.- {ECO:0000305|PubMed:30804501};
DE AltName: Full=C64 cluster protein NRPS5 {ECO:0000303|PubMed:25333987};
DE AltName: Full=Fg3_54 cluster protein NRPS9 {ECO:0000303|PubMed:30804501};
DE AltName: Full=Fusaoctaxin A biosynthesis cluster protein NRPS9 {ECO:0000303|PubMed:30804501};
GN Name=NRPS9 {ECO:0000303|PubMed:30804501};
GN Synonyms=NPS9 {ECO:0000303|PubMed:21585270};
GN ORFNames=FG10990, FGRAMPH1_01T20959;
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=21585270; DOI=10.1094/mpmi-02-11-0038;
RA Lysoee E., Seong K.Y., Kistler H.C.;
RT "The transcriptome of Fusarium graminearum during the infection of wheat.";
RL Mol. Plant Microbe Interact. 24:995-1000(2011).
RN [6]
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 [7]
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 [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
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 [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
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: Nonribosomal peptide synthetase; 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 -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|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).
CC Expression is also up-regulated during infection of barley
CC (PubMed:21585270). The fusaoctaxin A gene cluster is silenced by H3K27
CC trimethylation by the histone methyltransferase KMT6 (PubMed:31100892).
CC {ECO:0000269|PubMed:21585270, ECO:0000269|PubMed:23266949,
CC ECO:0000269|PubMed:25333987, ECO:0000269|PubMed:31100892}.
CC -!- DOMAIN: NRP synthetases are composed of discrete domains (adenylation
CC (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation
CC (C) domains) which when grouped together are referred to as a single
CC module. Each module is responsible for the recognition (via the A
CC domain) and incorporation of a single amino acid into the growing
CC peptide product. Thus, an NRP synthetase is generally composed of one
CC or more modules and can terminate in a thioesterase domain (TE) that
CC releases the newly synthesized peptide from the enzyme. Occasionally,
CC epimerase (E) domains (responsible for L- to D-amino acid conversion)
CC are present within the NRP synthetase. NRPS9 has a reduced A-T
CC architecture. {ECO:0000305|PubMed:30804501}.
CC -!- DISRUPTION PHENOTYPE: Leads to reduced virulence.
CC {ECO:0000269|PubMed:23266949, ECO:0000269|PubMed:30804501}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR EMBL; HG970334; CEF88261.1; -; Genomic_DNA.
DR RefSeq; XP_011325380.1; XM_011327078.1.
DR AlphaFoldDB; I1S2J4; -.
DR SMR; I1S2J4; -.
DR STRING; 5518.FGSG_10990P0; -.
DR GeneID; 23557864; -.
DR KEGG; fgr:FGSG_10990; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G20959; -.
DR eggNOG; KOG1178; Eukaryota.
DR HOGENOM; CLU_000022_2_12_1; -.
DR InParanoid; I1S2J4; -.
DR PHI-base; PHI:9043; -.
DR Proteomes; UP000070720; Chromosome 3.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Ligase; Phosphopantetheine; Phosphoprotein; Reference proteome; Repeat;
KW Virulence.
FT CHAIN 1..819
FT /note="Nonribosomal peptide synthetase 9"
FT /id="PRO_0000449945"
FT DOMAIN 722..798
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:30804501"
FT REGION 202..591
FT /note="Adenylation (A) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:30804501"
FT MOD_RES 759
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 819 AA; 89202 MW; 1CE04EA284492FAE CRC64;
MAPLNTYTST EVLLLDNACN DVHELGRALW SITVDRYHHR DEWTLTCLAE AHGRWDMTYR
LVSIQNATTI GQLLAAERLV ESPKDASDED NIFAFATTGS RLPVRTLLGR SSFILQLSEF
DGRPTAQVLF SGANNKGQAR ILLNVFHSLW ETHGSSPLNA ERPVCEVGGL SYEDVRILEL
VNSGRLAQQQ ECIHDVVLQH ALQAPTQHAV RAWDGNLTYH QLNDHADRIA TMLVSAGIGP
GDFIPSIMEK SYWTIVVILA TLKAGAVFVP IDPKCPASRI NGIFLQVWPK VYFTNLGPQM
RRKLNPSVAC VDNFAEIVQQ VQPGPLPPSR PDAIATCFFT SGSTGKPKGA IHDHSAIATG
IVDLLGPFHM DSRTSSMHFV SPSFDVSVTE IAATLYAGGC ICVPSEQGKL NDLNGQMRAL
GVTHAFLTPS VACQVKPSEV PTLQYIMLGG EPLGRATLEA LCEDVHLINV YGSTESGLWD
TASERLTLQS KPSNIGRSTG PRMWIVHPGN PGNLLPFGTV GEVMVESHCL ARGYIGNQPA
KTGFVPAPEW RHQLFPGMEQ GRFYLTGDLG SYNPDGSIML HGRKDTQAKI RGQRIELGEI
EHQFKAALPT SRVVAEVVTI GSRTMLAAFV ELSTAEDKTD IEPSVCVDSL SIRTAQAARL
GATPALSAAL PVYMVPEMYI PVNSIPLTMS GKTDRRRLRE LASTITTVQL EMINGVDDEK
EQPRNERERL IQATWAAVLQ RKASTIGIHD HFFKIGGDSL SAMKVVAAAR SRQLVINVGD
ILGHPTIASL AEFLSSSSTI SYATKGMANR DIQVTVTVL
