FUS1_GIBM7
ID FUS1_GIBM7 Reviewed; 3916 AA.
AC W7MLD7;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Fusarin C synthetase {ECO:0000303|PubMed:17121404};
DE Short=FUSS {ECO:0000303|PubMed:17121404};
DE EC=2.3.1.- {ECO:0000305|PubMed:17121404};
DE AltName: Full=Fusarin C cluster PKS/NRPS FUS1 {ECO:0000303|PubMed:22652150};
DE AltName: Full=Fusarin biosynthesis megasynthetase {ECO:0000303|PubMed:17121404};
DE AltName: Full=Fusarin biosynthesis protein 1 {ECO:0000303|PubMed:22652150};
GN Name=FUS1 {ECO:0000303|PubMed:22652150}; ORFNames=FVEG_11086;
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3125 / FGSC 7600;
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 [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17121404; DOI=10.1002/cbic.200600404;
RA Rees D.O., Bushby N., Cox R.J., Harding J.R., Simpson T.J., Willis C.L.;
RT "Synthesis of [1,2-13C2, 15N]-L-homoserine and its incorporation by the
RT PKS-NRPS system of Fusarium moniliforme into the mycotoxin fusarin C.";
RL ChemBioChem 8:46-50(2007).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RX PubMed=22652150; DOI=10.1016/j.fgb.2012.05.010;
RA Brown D.W., Butchko R.A., Busman M., Proctor R.H.;
RT "Identification of gene clusters associated with fusaric acid, fusarin, and
RT perithecial pigment production in Fusarium verticillioides.";
RL Fungal Genet. Biol. 49:521-532(2012).
CC -!- FUNCTION: Fusarin C synthetase; part of the gene cluster that mediates
CC the biosynthesis of the mycotoxin fusarin C (PubMed:17121404,
CC PubMed:22652150). Within the cluster, FUS1, FUS2, FUS8 and FUS9 are
CC sufficient for fusarin production (By similarity). The roles of the
CC other FUS members are yet undetermined (By similarity). The fusarin C
CC synthetase FUS1 is responsible for the condensation of one acetyl-
CC coenzyme A (CoA) unit with six malonyl-CoA units and the amide linkage
CC of the arising heptaketide and homoserine, subsequently releasing the
CC first intermediate, prefusarin, as an alcohol with an open ring
CC structure (PubMed:17121404). The cytochrome P450 monooxygenase FUS8
CC participates in multiple oxidation processes at carbon C-20 and is able
CC to use the FUS1 product as substrate, resulting in formation of 20-
CC hydroxy-prefusarin (By similarity). This reaction seems to be essential
CC before the 2-pyrrolidone ring closure can be catalyzed by FUS2,
CC generating 20-hydroxy-fusarin (By similarity). FUS8 is able to further
CC oxidizes carbon C-20 after ring closure, resulting in the formation of
CC carboxy-fusarin C (By similarity). As the last step, FUS9 methylates
CC the hydroxyl group at C-21 to generate fusarin C (By similarity).
CC Fusarin C can then rearrange to epi-fusarin C, the (z)-isomers, and
CC fusarin A and fusarin D (By similarity). {ECO:0000250|UniProtKB:S0EEY3,
CC ECO:0000269|PubMed:17121404, ECO:0000269|PubMed:22652150}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000250|UniProtKB:S0EEY3,
CC ECO:0000305|PubMed:22652150}.
CC -!- DOMAIN: FUS1 is an unusual polyketide synthase (PKS) fused to a non-
CC ribosomal peptide synthetase (NRPS) module to form a megasynthetase.
CC {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of fusarin C
CC (PubMed:22652150). {ECO:0000269|PubMed:22652150}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000305}.
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DR EMBL; DS022257; EWG52308.1; -; Genomic_DNA.
DR RefSeq; XP_018758499.1; XM_018900249.1.
DR SMR; W7MLD7; -.
DR STRING; 117187.FVEG_11086T0; -.
DR GeneID; 30068622; -.
DR KEGG; fvr:FVEG_11086; -.
DR VEuPathDB; FungiDB:FVEG_11086; -.
DR eggNOG; KOG1178; Eukaryota.
DR eggNOG; KOG1202; Eukaryota.
DR OrthoDB; 19161at2759; -.
DR Proteomes; UP000009096; Chromosome 9.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 2.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 3.40.366.10; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
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; IPR013120; Far_NAD-bd.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; SSF47336; 2.
DR SUPFAM; SSF51735; SSF51735; 2.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Isomerase; Ligase; Methyltransferase; Multifunctional enzyme;
KW Oxidoreductase; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW Repeat; Transferase.
FT CHAIN 1..3916
FT /note="Fusarin C synthetase"
FT /id="PRO_0000437356"
FT DOMAIN 2372..2449
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 3493..3570
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 12..443
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 548..869
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 935..1228
FT /note="Dehydrogenase (DH) domain"
FT /evidence="ECO:0000255"
FT REGION 1350..1584
FT /note="C-methyltransferase (CMeT) domain"
FT /evidence="ECO:0000255"
FT REGION 2092..2266
FT /note="Ketoreductase (KR) domain 1"
FT /evidence="ECO:0000255"
FT REGION 2482..2511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2522..2806
FT /note="Condensation"
FT /evidence="ECO:0000255"
FT REGION 2973..3385
FT /note="Adenylation"
FT /evidence="ECO:0000255"
FT REGION 3612..3833
FT /note="Thiolester reductase (R) domain"
FT /evidence="ECO:0000255"
FT ACT_SITE 182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2409
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3530
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 3916 AA; 430469 MW; 1575D18B68E23E2B CRC64;
MADNQSLPKE PIAIIGTSCR FPGGANTPSK LWDLLCEKRD VQSRIPNDRF NVDAFYSTNG
DKNGCTDVKR AYLLSEDIRV FDASFFKINP REAEAMDPQQ RLLLEAVYEA TEAAGLPMED
LKGSDTAVYV GCMTGDYHEM LMRDPQDMPK YMATGTARSI LSNRISYLFD WKGPSMTIDT
ACSSSLVAVY DAVTALRNGV SKIACAGGAN LILGPEMMIS ESKLHMLSPT GRSRMWDASA
NGYARGEGVA AIMMKTLSQA LADGDHIQGV IREIGVNSDG RTNGITLPSP EAQKFLIRQT
YKKAGLDVFK DRCQFFEAHG TGTPAGDPLE ARAIHEAFFT DGDIVSEPMY VGSVKTAIGH
LEGCAGLAGL IKALEAVKRG VIPPNQLFEN LNPALKPYVS NLRLPTESKP WPKLAPGSAR
RASVNSFGFG GTNVHAIIEQ FDHAQREASS ADGIISTPLV LSANSDLSLR KQIAHFAEAI
EHNDKGEVDR IIFTLAQRRS QLPLRAYFSG HGLQSIQQKL RDATAENAVL PFISQTVPPG
QPPRILGVFT GQGAQWPTMG REILKASPFA RTVMASLEES LASLAEPPIW TLTEQIMADK
DFSRLSEAAI SQPLCTAVQI MVVELLRKAG IAFNCVIGHS SGEITAAYTA GFLSATDAIR
VAYLRGVCAK LAGGGNGETG SMMAVGLSYE EASAFCEENF AGLVDVAASN APASTTLSGD
KPSIEEAKAS LDAQGTFARI LKVDTAYHSH HMNPCAQPYL EKLQAAGVKS LPGDDSVEWY
SSVLGERITA SLHSEALCDE YWVENMVNPV LFSVASELVA EANPPCHVAL EVGPHPALKG
PFNQTYKRAT GSPLPYHGTV TRNIHDVEAL SNSLGFLWSH LGKSAVDFTA YTQSFSPSIT
AMADGLPPYA WDHTQSFWRE SRKSLNYRQR TQPPHPLLGA RSVEDTADSM RWINYLRLDD
VPWLEGHKVE GQVVYPAAGY LVMAMEAARA IDASKEIQLT ELSDVHILSA IQLTEGSQAL
ETVFTLQVER NEPTFATASW TLSTPMSGRN DSWKSNAKGQ LRVEFSSLDD AARLPSRSKP
IASLTSVDME RFYSALANIG LEYTGEFKQL KSIDRQLGLA TAHVGQVVPD FPAMIHPALL
DGAFQSIFAA YCWPDDGSLQ APFVPTFFRS LRIANTSHLR HGEDLVIDSF LTNTNERELT
ADMDIFQSAE GQPVLQLQGL TCTSLLRPGP SNAKELYTKT EWEVDIASGI AQSDTQDQDT
ASDLELVDLC ERLSYFYLRE LNKAVGREEV SGFDWHYQRI FEWIDHLFPL IQSGRHPTIK
TEWSSDSRDW LMQQSARFPG RIDLQLIQAV GENLPAVVRK QTTMLEHMVK DDMLNRIYKF
GLGFERANVY LGRISKQIAH RYPRMNILEI GAGTGGATKG IMESLGTAFE TYTFTDISTG
FFEAAAEAFD HWADKMIFKP LNIESDPTDQ GFPQGHYDFI IASNVLHATK SLAVTMRNTR
KLLKPGGQLL LLEVTSDIVR VKLMMSGLSG WWLGGDDGRR YGPTIPVSQW DALLKQTGFS
GVDKTVNDFV DAEKYMTSVM LSQAVDDRME ILRQPRLASS HWLSSQSITV VGGHCQDIGK
DAMAIIHQMG HASSKPVIHH VGSFEELASS NIQTRSALVL EDLDEPILKD LTEDKLRGVQ
RLINESRQVL WVSRGCQKDE PFANMSIGMC RSLSSEYPHI HLQHVDIEGL VGPMTASLLV
DAFLQLMYRA SLKSDDLVWS IEAELVLRED KWFIPRVKSD EALNNQLNAS KMTIRSVKTL
HGDAVEIQQR SNQFVIAEPI PCIPVSASSP PVAITVTHSL LFPFQVGTKS SGYLCYGYID
SQPQTRVLAI SGVNRSKISV PPFFVWDLSS SEIDAADLLR KTALAITADR LLSDFEAGAT
VLIHESDENL GAALQWKAAE LDLNVILTTS ESSMERSTDS LFIHALAPER LVNHIMPQCT
KAVIDLSGRD YRIVDSPLRR CLPAHCKFHQ LQDILGNASQ GVNDPIIHGV RDASRSTLQL
SGDGPVINLS DLSNMRPSIK DYATIVEFSV DTTIPAVVQP LEGSQLFRSD KTYLLIGFTG
GLGKALCRWM VSCGVRHLAL TTRNVAAIDQ VWLQELRIQG AQVNLYQADV SDKAALSQAY
DQIVKEMPPV CGAANAALLL SDRTFTELKV KDFTQVFGPK VKGTQNLHEL LLDQKLDFFI
MFSSLASVVG NRGQANYAAS NLFMSAIAEQ RRAKGLAASV MHIGMVLGVG YVSSTGAYEA
TLRSSNYMAI SETDLLNMFS QAILVGQPSS THAPELITGL NRFSLEPEAQ KYFWRDNMRF
CHHTLEEEHQ ERTSTTKVSI SQRLSETKGT AEILAVVEEE FCTKLERLLQ AEAGSVKTSQ
SLLGLGVDSL VAAEIRSWFL KELEVDTPVL EILNTASITE LCSTVVSHLP TISEDTETKT
EVTKQAIKTL NVVETSTVVS SASPTENEPF TIRNSPNSTQ VTSESGVDEE TSIQSKIDRS
GPLSFAQERL WFLQQFLRDH STYNVTMHYH ISGPLRLHDL ERAFQQVIHR HESLRTSFFI
DPDTDLPTQA VLKDSSFRLE QKHNSTAKIE YKAMQGMSYD LENGNVVKAV IVPDSDGEFD
LIFGFHHIAL DGYSAQIMVR DLAMIYAGQT LSSKQQDYLD FAIAQKAAKV PYTTLAYWRS
ELEDLPPTLT VFDFAETKTR IPLTDYTTRA LERRLSIEQS RSIKAVAKRL DVTPFHVHLA
TLQVVLSDLA SANDLCIGIT DANKNDATHI DTVGFFVNLL PLRLKLSSSQ TLADLVANAK
SKANGALSHS DMPFDVLLDE MKLPRSTTHS PLFQVVMNYK MGSTQKVPLA DCQAQLVAFE
DANNPYDLTF DIETYYDGSA SISVKTQEYL YSESELSFVL DNYVEKLDLF TSEPSQTVDQ
ICKPTAEQIG KALTLGRGER IPSPRLETLS HYFEKCVVNQ PDDVALVTDK GQALTWSQLK
ALVNQIAMAL VEAGAKQDSQ VGVYCDPSMY ILPTLIAIAE IGGVYVPLDT QNPIKRLQLM
VDDCQADVLL IDDSTATLSL ELETKAKMIN VNTIKAGPSN TFHLDNRARG NGMGYIFYTS
GTTGVPKAVA LTHTSLVHHF DGFIHCNNLN KCRMLQQAPL GFDMSLTQMT LAIMLGGTLI
VASSETRKDP TQLAQLMLDE KVTHTFMTPT LALSVIHHGY EYLRQCVDWE HASLAGEAMT
TRVTSEFKRL GLRNLELCNG YGPTEITIIA TCGSNELGDT LRDTHNPSIG RALPNYSCYI
LDENMQPVRP GLAGELVIGG AGVAIGYLNR QDLTEAKFLS DPFAPPEDVA RGWTRMYRTG
DKARFLSDGR LCFLGRIAGD SQIKLRGFRI ELQDIASTIV KASDGKVPEA AVSLRGEGDS
AYLVAFVILS QFNRPSDEKG YLKQLLEELS LPRYMKPAKI ISISQLPMNA SGKLDQYALD
ALPVSYEKDI VDKPLTETQE RLKLGWLKAL PFVDAAIGPD TDFFSAGGNS LRIVSLREYI
TREFGVTVSV FDLFQASTLG EMAAKIDGFT TQEATTISID WEEETRIDAD LNIVGVQEPL
PSEATNGLQV ALTGATGFLG VSILETLLED KRVSKVHCLA VRSSSNTSDP VFSSSRVACY
PGDLSLPRLG LSQEQFDQLA NAVDRIIHNG ADVSFLKTYQ SLQRSNVSSS RELARMAITR
RIPMHFVSTG GVVQLTGQDG LDEVSVIDST PPNDGSLGYV ASKWASEAIL EKYASQYNLP
VWIHRPSNIT GPNAPKADLM QNIFHYSAKT ASLPDLASWS GCFDFVPVDV VAAGIASSIY
ETQETVAYKH HCGTEKISVE DLPSYLEAKH GKIETVSIEE WLERSKAAGL DEVTAVLVEK
TLSRGGIVPW LRREAN
