NPS6_GIBZE
ID NPS6_GIBZE Reviewed; 2071 AA.
AC I1RIV2; A0A098DKX4;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Nonribosomal peptide synthetase 6 {ECO:0000303|PubMed:17056706};
DE Short=NPRS 6 {ECO:0000303|PubMed:17056706};
DE EC=6.3.2.- {ECO:0000305|PubMed:17056706};
DE AltName: Full=Extracellular siderophore synthetase {ECO:0000303|PubMed:17056706};
GN Name=NPS6 {ECO:0000303|PubMed:17056706};
GN ORFNames=FG03747, FGRAMPH1_01T13607;
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, DISRUPTION PHENOTYPE, INDUCTION, DOMAIN, AND PATHWAY.
RX PubMed=17056706; DOI=10.1105/tpc.106.045633;
RA Oide S., Moeder W., Krasnoff S., Gibson D., Haas H., Yoshioka K.,
RA Turgeon B.G.;
RT "NPS6, encoding a nonribosomal peptide synthetase involved in siderophore-
RT mediated iron metabolism, is a conserved virulence determinant of plant
RT pathogenic ascomycetes.";
RL Plant Cell 18:2836-2853(2006).
RN [5]
RP FUNCTION.
RX PubMed=17043871; DOI=10.1007/s00294-006-0103-0;
RA Tobiasen C., Aahman J., Ravnholt K.S., Bjerrum M.J., Grell M.N., Giese H.;
RT "Nonribosomal peptide synthetase (NPS) genes in Fusarium graminearum, F.
RT culmorum and F. pseudograminearium and identification of NPS2 as the
RT producer of ferricrocin.";
RL Curr. Genet. 51:43-58(2007).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=17601875; DOI=10.1128/ec.00111-07;
RA Oide S., Krasnoff S.B., Gibson D.M., Turgeon B.G.;
RT "Intracellular siderophores are essential for ascomycete sexual development
RT in heterothallic Cochliobolus heterostrophus and homothallic Gibberella
RT zeae.";
RL Eukaryot. Cell 6:1339-1353(2007).
RN [7]
RP FUNCTION.
RX PubMed=20507510; DOI=10.1111/j.1364-3703.2007.00401.x;
RA Greenshields D.L., Liu G., Feng J., Selvaraj G., Wei Y.;
RT "The siderophore biosynthetic gene SID1, but not the ferroxidase gene FET3,
RT is required for full Fusarium graminearum virulence.";
RL Mol. Plant Pathol. 8:411-421(2007).
CC -!- FUNCTION: Nonribosomal peptide synthetase; part of the gene cluster
CC that mediates the biosynthesis of hydroxamate-containing siderophores
CC that play a critical role in virulence (PubMed:17043871,
CC PubMed:17601875). Gibberella zeae produces extracellular coprogen-type
CC siderophores as well as the intracellular siderophore ferricrocin
CC (PubMed:17056706). The role of extracellular siderophores is to supply
CC iron to the fungus during plant infection, and the intracellular
CC ferricrocin is required for intracellular iron distribution and storage
CC with a crucial role in ascus and ascospore development
CC (PubMed:17056706, PubMed:17043871, PubMed:17601875). SID1 catalyzes the
CC conversion of L-ornithine to N(5)-hydroxyornithine, the first step in
CC the biosynthesis of all hydroxamate-containing siderophores
CC (PubMed:20507510). The assembly of extracellular coprogen-type
CC siderophores is performed by the nonribosomal peptide synthetase (NRPS)
CC NPS6 whereas the intracellular siderophore ferricrocin is assembled by
CC NPS2 (PubMed:17056706, PubMed:17043871, PubMed:17601875).
CC {ECO:0000269|PubMed:17043871, ECO:0000269|PubMed:17056706,
CC ECO:0000269|PubMed:17601875, ECO:0000269|PubMed:20507510}.
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000269|PubMed:17056706}.
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 (By similarity). Each module is responsible for the recognition
CC (via the A domain) and incorporation of a single amino acid into the
CC growing peptide product (By similarity). Thus, an NRP synthetase is
CC generally composed of one or more modules and can terminate in a
CC thioesterase domain (TE) that releases the newly synthesized peptide
CC from the enzyme (By similarity). Occasionally, methyltransferase
CC domains (responsible for amino acid methylation) are present within the
CC NRP synthetase (By similarity). NPS6 contains a degenerate A domain
CC (dA) in the second module and has the following architecture: A-T-C-dA-
CC T-T-C (PubMed:17056706). {ECO:0000250|UniProtKB:A0A144KPJ6,
CC ECO:0000305|PubMed:17056706}.
CC -!- DISRUPTION PHENOTYPE: Leads to increased sensitivity to oxidative
CC stress and raduces the virulence toward wheat plants (PubMed:17056706).
CC {ECO:0000269|PubMed:17056706}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR EMBL; HG970333; CEF78606.1; -; Genomic_DNA.
DR RefSeq; XP_011321944.1; XM_011323642.1.
DR AlphaFoldDB; I1RIV2; -.
DR SMR; I1RIV2; -.
DR STRING; 5518.FGSG_03747P0; -.
DR GeneID; 23551040; -.
DR KEGG; fgr:FGSG_03747; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G13607; -.
DR eggNOG; KOG1178; Eukaryota.
DR HOGENOM; CLU_000022_60_2_1; -.
DR InParanoid; I1RIV2; -.
DR PHI-base; PHI:1007; -.
DR Proteomes; UP000070720; Chromosome 2.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.10; -; 2.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.559.10; -; 2.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
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; PF00668; Condensation; 2.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 2.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 2: Evidence at transcript level;
KW Ligase; Multifunctional enzyme; Phosphopantetheine; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..2071
FT /note="Nonribosomal peptide synthetase 6"
FT /id="PRO_0000444388"
FT DOMAIN 762..838
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1553..1629
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 228..631
FT /note="Adenylation"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:17056706"
FT REGION 878..1294
FT /note="Condensation 1"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:17056706"
FT REGION 1689..1980
FT /note="Condensation 2"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:17056706"
FT MOD_RES 799
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1590
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2071 AA; 228310 MW; 5E8D63EF2FD59AFE CRC64;
MTELDLSAEP NVPQTKTVRH NVPVLRKHHE QDAQELEILL LAWSLLLYRH NHGNHVEFSW
GLTEIGSSTC RTFTLNTAKL QWDGSNIVAS ELEVFKTYTQ QQLQSEVPFK RDQYKLFFND
EPATGDLVNY ITEDGDISVN WGNVQIQATL VDDALCLRPT WREPLGAEFL ANHLAQAFVE
VLNTTLADPD ATLSSVLPLG KLDKSVIWNW NKDLPPPVPE CIHTLISEQV RLRPDAQAIC
SWDGDLTYAE MDNLSTLLAQ HLINLGVKNG DIVPLCFEKS RWTTVGVMGV IKAGAAFVLM
DPSQPIQRRQ VMAQQVKATH ILTSRDQAKY GPEIAPEAKH VIVDTETLDS LAKTIEDPSR
ELPQVPPESL LYIIFTSGST GTPKGVMLSH ETYTASALAR STGIGYSSIS RSLDFTSYAF
DVSIDSILCT LIRGGCLCIP TDMDRVNDLS GAIRRLKVNM VNITPSVARI LDPDIIPSLN
SLGIGGEACS AGDIAIWGQH TRIVIGYGPA ECTIGCTVNP SAAGKPYVSM GPGTGACIWL
VDPDDHNKLV PVGAVGELLI EGPIVGQGYL GDPEKTKEAF ISDPDFLLAG ADGIPGRQGR
LYKSGDLVRY DPDGENGFIF VGRKDTQIKL RGQRVELGEI EHHIKNLLPS GAEVVAEIIA
PRNQNKESML VAFVADREAK DEGDARQIDF PPRFREALEV LNDKLSKVVP VYMVPTQYIT
LSKIPYLVSG KTDRKSLRAL GAEISANMQA SAAANESSEI REPQSEAELF LRDSWCRLLG
LENKQVSTTH NFFTSGGDSV LAMKLVPIVR DWGYTLSVAD IFNYPVLSDM ANSMQKGDSS
KGVDMQIPEF SLLKDDMDRE ALCAEAAHNS GCDVSAIEDI YPCAPMQEIH MAFYTRSKEN
YVAQRIADIP ASSSIDKLKS AWNVVYKESP ILRTRIVEFK QHGFMQVVVN EALQWEEVDS
SLEDFIEKDK KESMSPGAPL SRFAIVTDKA LDKRYFVWTA HHAIYDGWST DLIVEHARAA
YKGQEVSRPA QFKHFIRYLA EDSRESSKAY WKTQLAGATG PQFPSLPSRS YIPDPTSLTE
RFIKLDKAAK SDITIATVIR AAWALLASQY SMSDDVVFGE TFMGRTIPLP GAELIEGPIL
ATVPVRIRLD LTTTVQDFLR AVQEQSVKRA AHEHLGIQHI RRLSDDAQIA CEVTMGLVVQ
PQDPDPTETE NDALPSFRGG DAALEALHFN SYPLMLAVSM QKTGFRLLAS FDSELLSHVQ
VERVLSQFEV AINQLRGDMS RSLNELTCLG EEELGQIWEA NKHAPVSPKD ISRFLSTGDK
YPTVQYVPWV VQPGNEKLLM PLGSTGELLL EGIASAGDDD DVVDAPEWLK EGAMGYPGRQ
GKLVRTGDLV KYADDMSLVF IGRKDAMTSV DGRVVDLNAT NIELNRLLPS NTKAVSRLVV
PKGSNSQTPV VVALVQETSA KDTQLLKLGL DISDASMPLS QAVSVELATA IIGLNKAMVE
TLPPYAIPSI CIPLDNSADI DSIDTIVENI TLSLVVELRK SFASLKKTIA DTTVLTTKER
VLRASWSKFL GIEEEKLALD DNFFRLGGDS IVAMRMVSAL RQDGYRLSVA SIFQNMQLRG
MADSLAEIST ESVEAAKEYT AFSMLDTNDV DSFLAKVIRP QLADPKWKIK DVLHATGPQA
GDVKQSVFAP RSSVQYNMLY LDQSIDTARL VDSFQYLVSQ HAILRTVFVE NEGQTLQVVL
DDLKVPVTEQ NVEGSIDAAA KQLAVSDINS SIDLTHGSSF IRLFVLRGES ENALVIRISH
AQYDGVSLPE LLRQLELRYR GLEIPSSEPF ETYIQHLSAA KPQNVEFWRK TLQGSSYTEI
APAADPQKKT AFMTKDVDIS GASPNTTHAM LLTAGWAKVL SQHLNVSDVT FGGIVSGRDV
DVAGIDTIMG PCYQYQPVRV KFESNWTATD LLDSVRSQSL EGSQRATLSF QEVLKECTNW
PAGTPFYGSF TNHLNKEFFD SIPFAGTKCR VDYSIPHPEP ATPPRVVSFL EDGRTQIGIE
ADEERREFWE ARLGELAKVI EGFVKNPQAL I
