ID   FUSA2_GIBZE             Reviewed;        4423 AA.
AC   I1RVD9; A0A098DC07;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   23-FEB-2022, entry version 64.
DE   RecName: Full=Nonribosomal peptide synthetase 7 {ECO:0000303|PubMed:25412204};
DE            Short=NRPS 7 {ECO:0000303|PubMed:25412204};
DE            EC=6.3.2.- {ECO:0000305|PubMed:25412204};
DE   AltName: Full=Fusaristatin A biosynthesis cluster protein NRPS7 {ECO:0000303|PubMed:25412204};
GN   Name=NRPS7 {ECO:0000303|PubMed:25412204};
GN   ORFNames=FGRAMPH1_01T09373, FGSG_08209 {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, DISRUPTION PHENOTYPE, 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: Nonribosomal peptide synthetase; part of the gene cluster
CC       that mediates the biosynthesis of the lipopeptide fusaristatin A
CC       (PubMed:25412204). Fusaristatin A consists of a polyketide chain linked
CC       to three amino acid residues glutamine (Gln), dehydroalanine (dehydro-
CC       Ala), and beta-aminoisobutyric acid (PubMed:25412204). The biosynthesis
CC       starts with formation of a linear polyketide chain by the highly
CC       reducing polyketide synthase PKS6 (PubMed:25412204). The gene cluster
CC       does not contain an acyl-CoA ligase or an acyl-transferase, and it is
CC       therefore 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   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:25412204}.
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 (By similarity). NRPS7 has the
CC       following architecture: C-A-T-C-A-T-C-A-T-Cy. The last condensation
CC       domain (Cy) could be responsible for cyclization of the final product
CC       (Probable). {ECO:0000250|UniProtKB:Q4WAZ9,
CC       ECO:0000305|PubMed:25412204}.
CC   -!- DISRUPTION PHENOTYPE: impairs the production of fusaristatin A.
CC       {ECO:0000269|PubMed:25412204}.
CC   -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR   EMBL; HG970333; CEF76489.1; -; Genomic_DNA.
DR   RefSeq; XP_011320598.1; XM_011322296.1.
DR   SMR; I1RVD9; -.
DR   STRING; 5518.FGSG_08209P0; -.
DR   GeneID; 23555234; -.
DR   KEGG; fgr:FGSG_08209; -.
DR   VEuPathDB; FungiDB:FGRAMPH1_01G09373; -.
DR   eggNOG; KOG1176; Eukaryota.
DR   eggNOG; KOG1178; Eukaryota.
DR   HOGENOM; CLU_000022_60_0_1; -.
DR   InParanoid; I1RVD9; -.
DR   Proteomes; UP000070720; Chromosome 2.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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; -; 3.
DR   Gene3D; 3.30.300.30; -; 3.
DR   Gene3D; 3.30.559.10; -; 5.
DR   Gene3D; 3.40.50.12780; -; 3.
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; 3.
DR   Pfam; PF00668; Condensation; 4.
DR   Pfam; PF00550; PP-binding; 3.
DR   SMART; SM00823; PKS_PP; 3.
DR   SUPFAM; SSF47336; SSF47336; 3.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 2.
DR   PROSITE; PS00455; AMP_BINDING; 3.
DR   PROSITE; PS50075; CARRIER; 3.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE   3: Inferred from homology;
KW   Isomerase; Ligase; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW   Repeat.
FT   CHAIN           1..4423
FT                   /note="Nonribosomal peptide synthetase 7"
FT                   /id="PRO_0000445374"
FT   DOMAIN          1533..1609
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          2642..2718
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          3731..3804
FT                   /note="Carrier 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          572..986
FT                   /note="Condensation 1"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:25412204"
FT   REGION          1007..1404
FT                   /note="Adenylation 1"
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:25412204"
FT   REGION          1657..2066
FT                   /note="Condensation 2"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:25412204"
FT   REGION          2102..2499
FT                   /note="Adenylation 2"
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:25412204"
FT   REGION          2764..3170
FT                   /note="Condensation 3"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:25412204"
FT   REGION          3205..3609
FT                   /note="Adenylation 3"
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:25412204"
FT   REGION          3875..4278
FT                   /note="Condensation 4"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:25412204"
FT   REGION          4288..4312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        4298..4312
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1570
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         2679
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         3765
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   4423 AA;  488395 MW;  E80EB1E8F4402D91 CRC64;
     MQGGPVICNG IPSVTISILP HPRSRARTSL LLRRGGALGP GSGCMSDRLF TTPDMRKNRQ
     RLTLAASVVL KKEENEIDLE KSLVEQGGDM LSGVFFAGQC RELGLIVDIA NASSMSLRDM
     ALQLVESNPE LLRPSTAMDC RSASVPHTLL QSLYRNFGAS TGVTLDVDIP LTLEDVTKML
     QRLVERHPIL GSTAEPNDKT SYVFSNTVPS PILVSFESDK THAEMRMLQE DSKSKVAVFS
     VMAFGEESRI TNLSFVADNA AIDAQSWSIL LHDIQAFPAG FNDLTTQSNT FPNWIESAFR
     VTDTTVETAG TTKLPIHSEM SAEDSSPALS SCVFTLNPEL TQAIQSEACH RTLRTEVQDV
     MFGALASTFG TQLPASARYL EIKDGRPQDE GNAWNSVIGC FDEIFELAYE CHGDIIDACR
     SAKDSRKQSS LSPVHYASCR YNLILDTTWL KACIGTSSTG KMRLMDNEPG RYAAEALVKS
     MGGLCMTPFW QGTGLSFLVV SSTDFGSDED LKLNSEMFIN HVQHISETLP NRSPWPTLSD
     FPHVSFDYPS LDRMFQQKLL QITQTPLADI HNIYPCTSIQ ENMLMGNSLD KDAYVCSFTA
     RATTSGAFTH FDAAKWAEAW GRVVEKHSSL RTIFIESEGR PGHFEQVILK SVAAPVDIMT
     GPSVPSKIEF QDFSVPHHLA IIQEGPGRCL MILTMSHAIT DGHSAEVLLG DLCAEAVQTD
     GTGEEAFAYS EFALTEYQST NTEVSDYWQD YLLKTQETIL PVTREKSDFH DFNTVHSTMP
     VNVSSMDRIC RRHNINLASV CQFAWGVVLR SRLGVDGVCF SYISSLRNKP LKGIMTAVGP
     LITTLLCSMN LEGERPVLDA IRAVDSEYVE SLSHEKELYN ITSPRRWCNT VMSFRRRLVQ
     DDGGIPGLSY KLVKAFSPTN YDFSLIVSAG QSDLDIMLDY WGSRMDRDNA QSLLQIFQEV
     LHSIFRDIDS TVSGLDLISQ DDKNRILERN RLVPKGLNRC VHELVNERIQ KQPSAVAIDA
     WDGSLTYSEL DNLTSRLAQY LSNIGVGPEV PVGICMDKSK LVPVTVLAIL QAGGAVLPIG
     VEEPEARVEA ILADATPVAI VGDGRQVTRL SELGTQVLNV VDILADMSSS LPSSTSKQET
     RATPDTTAWI FYTSGSTGTP KGVLVEHQAL ATSMRAHGVA LKVLPEDRVL QFAAHTFDVS
     LSELFTTLIF GGCVCIPDET NRVNDLAGSV HGLQANVLSL TSSMASTIRP RDVPMVRKLV
     LFGEEVKASV VEAWLGKADI YNAYGPTESS IFASVSKPFQ SVDDLSNIGY PMDVNFWVTD
     PQNPGRLCPP GSPGELLIEG PLLARGYLND DNKTSTAFIQ DPSFASLLGL EKGRRFYRTG
     DLVRQNSDFS MSYLGRRDTQ VKIRGQRLDV SEVEHWITAS LEGAVRVVVD LLPGAILFAA
     VEFSPHAVVV VSGDKTILQT SDEFRHRFSQ LKNALQGKLP SYMLPTFYVP FRRIPLTSSA
     KTDRKMVRLL VSQLDTIILQ QYISNDSNES DDLPLTETEQ KLKVLWANVL NVTHSSIGAG
     DHFLYRGGDS LMAIKLVEQA RLESISMTVK DVLSFPRLQD LARTIDERNE VGIISSAQMA
     NQHDPPAFSL WKPSSSDRET ELADIAMQCG LGTEDIEDVY PCTSLQESML AATQQRPTAY
     IVRQMYSLSD SIDLSHFRKI WDVLVQQAPV MRTHILLGQR SGSLQVLSKK PLTWYNHDDL
     DEYVAADQAR AMATGQPLMR LALVQDKSKG VRYFVWTAHH SVYDGWSAQL IYKRLAALYL
     YEEVPTAVPF TRFIEYQQRT KDDSDINLGS YWRGQLGGDV PSAFPSMPSP FYQPKPVSLH
     RSEIDTLSFK PSKYGFSLAD ILRAGWAMTL GQYLGTNDVV FGAILSGRNA PVAEITQLIA
     PTITTVPVRV TVDREAKVSW YLAAIQSQAV EMIPYEHTGL DEIKRLCPDL QPATDVNHAF
     VIEPPYAKDG DAHTILPGLE LVDTALDTFD TFALTIQCQL PSKQGGSIKV EARFDAKVVS
     DAQVTVLLRQ FEHWVSQFLD ETHHETQLKS LEEITSADLA QIKKQNSRIP VRDMVCLHHL
     IRDVAKEQPD SPAVCAWDGD FTYEELWTNA RRLAQHLSNL GVGPKSRVAV CMDKSRWTVA
     SILGILESGG VVVMLRSQSP LEQAKALVAD CQATAMLVNA GHTARFAGSG PRIVEVNDAL
     LASLPDPTVS GPICPALNPG HPAWIVYTSG STGLPKGCLL IHGGLATSLP AHGRATRWHK
     ESRTLQFASH EFDVTLQEIM TTLIFKGCVC IPSEDQRINS LSQAIRDMNV TQMVLTPTVA
     SMINPVDVPC IVQLQVAGEL IKPSVVERWI DHAEVVNIYG PSECSVYSSC GTPMQTIEDA
     PVIGYPLDNC NFWVTSTTDH NRLCPIGIPG ELLIENSWQA WGYVNNPELT AQCFVVEPGF
     IKQLGLDGSG RRMYRTGDLV QQNPNGSYTY IGRMGSEVKF RGHRVDLGRI EYWIGKLLEG
     VQTIAVDLVE LDTGKKANDL VAVIDFTDDC DLFDLDQTED IDGVAILTPS TKIRKALCRL
     RDGLTDKLPS YMVPTAFMPW KKIPFTSSGK TNRKAIRQLL TNLEAGSSLL QRYLADGDVK
     EVPQTRIGKK LQQLWAEVLS VKVDSIGSQD HFTRLGGDSL AAMKLVASAR QVGLELSVTS
     IFTYPVLEDC ARILEADQDS SLVKLPEEDP APFELMPEDW STGGFEDRLA DFAAQCRVAP
     SQIEDVYPCT PMQEALFAIT ARNPTAYTYR QVFRASGEDV DMVRFQTAWE TVASILPILR
     TRIVLDQSGF LQTVIDQPLI WHIGGDLDSY IAADKLVGFE PGTPLLRCAI VEGGGAKYFV
     LTTHHSMFDK WSIEKIMYRY LIPAYFGQQL PEAVPFPRFV RHVLNIDMDS ASQFWTQKLE
     DDEPFTEFPS LPSVGFYEPK PTGLLSQTFR IDGVNKLETP FPSLLRAAWA LTVSQYAGAE
     DVMFAVNLSG RSAPVADISE LAAPTFTTVP VRVRINRSQR VRDFLDGLHR ETIAMVPFEH
     VGLRNIKRFV PTFNPSDLRH LFLVHTAADD TLDDPSFRLP GFEQVHQKAE TLDDYPLTIL
     CKLDDHKGEA EVVARFDSTV IPADQIQSVL RQFEHNVVQL AASASSDDQT VGGLPLVSSY
     DLDRISAWNV TGPPSLGCVH DLFIRSLETR PDSQAVCSWD GEFTYRELDQ AARILAQLLV
     AEGGVGTEVA VGLCMDKSRW AMVAVLAILY AGGAVVPLGV DLPPERISVI LQDSSPTMVL
     CDEAKADRFR SLGCKIAVVN ETEIDGVAKS YDGYNPNIPS TSVSAENMAW IIYTSGSTGV
     PKGVTLEHGG IYNIILNKGT TLGFDSTTRT FQFAAFTFDV SIADPLMAWA FGGCVCLPSE
     DERMNDLVGS INRLNANFAL LTASTAALIT PSEVPRMTKL LLGGESNTPS LMEKWLLDSN
     ITVGNSYGPA ECSITSTINA RVTDKNGCNI IGNPIQGTQA WIADFHDCNR LVPIGAVGEL
     LIEGPHVARG YRNDAVKTMA AFITDPRFTT DVGPKRHGRR MYRSGDLVRY TSDGNIEFLG
     RGDSQIKIRG QRVDLGEIES CIVKLVPKVR TALVEYLHLS EDQRALIAAL EFHNADKDQD
     VEGLATWLKE SLAQQLPAYM IPRAYLQIDM IPKTVSGKTN RKAIRQFMMN KYMQIADENS
     LNDFQTGKVD TESEYITRTL WAAVLGVDAD RIDRHDNFFD IGGDSIIAMK LVAAAKVKGF
     QIRVLDIFEN PVLFKMAVVA QHQTEMALEA VSPPPYYPFQ LLDSDDNDID TILEEFVCPV
     TGTGKESIQD VFPAPDAIAF GVAGALTAAQ PEVNTFVLDA EGDLDLVRLQ QSCVLLAHHI
     EAFRTAFAFD LRSGRLLQIV LKSYQHNVLV VRTRESLEDA TERLFEKDIY HEPFRLGTPL
     VSMTILQEHN SRNTRILLRM SHAIYDAMSL PIILRTLRSL YHKQDAYKPP LFSFAEYVAD
     LNRHTGNTSY NYWRNLLQGS TMTEVIPTAA YGGQNPVQMA FTNAKMIAVR KSKGDGITTS
     TIISCAWAHV LAQYTGKPDV VFGDTISGRN LVDPSISSTV VGCCATNVPM RVRFAGDSGE
     HSILQLLNQV RDQQRSRIPH EGVGVRSLIH ECTDWSPEAR FTSVVNHRPA NDPAVKSISN
     QIDFKVSTIT TENKPFMTWY DLAVISQENN GHVEMSLGYS TTGFHPETAQ SLLEDLADTV
     QILLNAVSSQ DEKLALLGTE VMPRSSSKLT KLQRVNSPKE QTLRKDKPTN GVFSDKPDDA
     TLSVLDTIWF SIFTSNRAGV GTLASDELTP DLRYLPFYKV GGDLLDAAWF IALIQRRVKT
     SGRESNGDGI LASHNQLTVD DVLRHPSVVE FAGLLKQKQV ELN