FUS1_GIBF5
ID FUS1_GIBF5 Reviewed; 3916 AA.
AC S0EEY3; J7GLW4;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Fusarin C synthetase {ECO:0000250|UniProtKB:W7MLD7};
DE Short=FUSS {ECO:0000250|UniProtKB:W7MLD7};
DE EC=2.3.1.- {ECO:0000269|PubMed:23932525};
DE AltName: Full=Fusarin C cluster PKS/NRPS FUS1 {ECO:0000303|PubMed:23932525};
DE AltName: Full=Fusarin biosynthesis megasynthetase {ECO:0000250|UniProtKB:W7MLD7};
DE AltName: Full=Fusarin biosynthesis protein 1 {ECO:0000303|PubMed:23932525};
GN Name=FUS1 {ECO:0000303|PubMed:23932525};
GN Synonyms=fusA {ECO:0000303|PubMed:22865073}; ORFNames=FFUJ_10058;
OS Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS and foot rot disease fungus) (Fusarium fujikuroi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1279085;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831;
RX PubMed=22865073; DOI=10.1128/aem.01552-12;
RA Diaz-Sanchez V., Avalos J., Limon M.C.;
RT "Identification and regulation of fusA, the polyketide synthase gene
RT responsible for fusarin production in Fusarium fujikuroi.";
RL Appl. Environ. Microbiol. 78:7258-7266(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831;
RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA Wiemann P., Sieber C.M.K., von Bargen K.W., Studt L., Niehaus E.-M.,
RA Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA Proctor R.H., Muensterkoetter M., Freitag M., Humpf H.-U., Gueldener U.,
RA Tudzynski B.;
RT "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT novel metabolites.";
RL PLoS Pathog. 9:E1003475-E1003475(2013).
RN [3]
RP INDUCTION.
RX PubMed=20572938; DOI=10.1111/j.1365-2958.2010.07263.x;
RA Wiemann P., Brown D.W., Kleigrewe K., Bok J.W., Keller N.P., Humpf H.U.,
RA Tudzynski B.;
RT "FfVel1 and FfLae1, components of a velvet-like complex in Fusarium
RT fujikuroi, affect differentiation, secondary metabolism and virulence.";
RL Mol. Microbiol. 77:972-994(2010).
RN [4]
RP FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RX PubMed=23932525; DOI=10.1016/j.chembiol.2013.07.004;
RA Niehaus E.M., Kleigrewe K., Wiemann P., Studt L., Sieber C.M.,
RA Connolly L.R., Freitag M., Gueldener U., Tudzynski B., Humpf H.U.;
RT "Genetic manipulation of the Fusarium fujikuroi fusarin gene cluster yields
RT insight into the complex regulation and fusarin biosynthetic pathway.";
RL Chem. Biol. 20:1055-1066(2013).
CC -!- FUNCTION: Fusarin C synthetase; part of the gene cluster that mediates
CC the biosynthesis of the mycotoxin fusarin C
CC (PubMed:22865073,PubMed:23932525). Within the cluster, FUS1, FUS2, FUS8
CC and FUS9 are sufficient for fusarin production (PubMed:23932525). The
CC roles of the other FUS members are yet undetermined (PubMed:23932525).
CC The fusarin C synthetase FUS1 is responsible for the condensation of
CC one acetyl-coenzyme A (CoA) unit with six malonyl-CoA units and the
CC amide linkage of the arising heptaketide and homoserine, subsequently
CC releasing the first intermediate, prefusarin, as an alcohol with an
CC open ring structure (PubMed:23932525). The cytochrome P450
CC monooxygenase FUS8 participates in multiple oxidation processes at
CC carbon C-20 and is able to use the FUS1 product as substrate, resulting
CC in formation of 20-hydroxy-prefusarin (PubMed:23932525). This reaction
CC seems to be essential before the 2-pyrrolidone ring closure can be
CC catalyzed by FUS2, generating 20-hydroxy-fusarin (PubMed:23932525).
CC FUS8 is able to further oxidizes carbon C-20 after ring closure,
CC resulting in the formation of carboxy-fusarin C (PubMed:23932525). As
CC the last step, FUS9 methylates the hydroxyl group at C-21 to generate
CC fusarin C (PubMed:23932525). Fusarin C can then rearrange to epi-
CC fusarin C, the (z)-isomers, and fusarin A and fusarin D
CC (PubMed:23932525). {ECO:0000269|PubMed:22865073,
CC ECO:0000269|PubMed:23932525}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:23932525}.
CC -!- INDUCTION: Expressed under high amounts of nitrogen via regulation by
CC GLN1 (PubMed:22865073, PubMed:23932525). Moreover, components of the
CC fungal-specific velvet complex VEL1, VEL2 and LAE1 act also as positive
CC regulators of expression (PubMed:20572938, PubMed:23932525). Finally,
CC expression is induced under acidic conditions in a PACC-independent
CC manner (PubMed:23932525). {ECO:0000269|PubMed:20572938,
CC ECO:0000269|PubMed:22865073, ECO:0000269|PubMed:23932525}.
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:22865073, PubMed:23932525). {ECO:0000269|PubMed:22865073,
CC ECO:0000269|PubMed:23932525}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AFP73394.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JX308619; AFP73394.1; ALT_SEQ; Genomic_DNA.
DR EMBL; HF679031; CCT73260.1; -; Genomic_DNA.
DR SMR; S0EEY3; -.
DR STRING; 5127.CCT73260; -.
DR PRIDE; S0EEY3; -.
DR EnsemblFungi; AFP73394; AFP73394; AFP73394.
DR EnsemblFungi; CCT73260; CCT73260; FFUJ_10058.
DR VEuPathDB; FungiDB:FFUJ_10058; -.
DR HOGENOM; CLU_000022_37_5_1; -.
DR BioCyc; MetaCyc:MON-19357; -.
DR Proteomes; UP000016800; 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_0000437355"
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..866
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 1347..1575
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 2487..2510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2522..2806
FT /note="Condensation"
FT /evidence="ECO:0000255"
FT REGION 2975..3385
FT /note="Adenylation"
FT /evidence="ECO:0000255"
FT REGION 3612..3833
FT /note="Thiolester reductase (R) domain"
FT /evidence="ECO:0000255"
FT COMPBIAS 2487..2508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 431028 MW; 983533C58D311E9D CRC64;
MAGNQYLPKE PIAIIGTSCR FPGGANTPSK LWDLLCEKRD VQSRIPNDRF NVDAFYSTNG
DKNGCTDVKN AYVLSEDIRV FDASFFKINP REAEAMDPQQ RLLLEAVYEA TEAAGLPMED
LKGSDTAVYV GCMTGDYHEM LMRDPQDMPK YMATGTARSI LSNRISYLFD WKGPSMTIDT
ACSSSLVAVY DAVTALRNGV SKIACAGGAN LILGPEMMIS ESKLHMLSPT GRSRMWDASA
NGYARGEGVA AIMMKTLSQA LADGDHIQGV IREIGVNSDG RTNGITLPSP EAQKVLIRQT
YKKAGLDFFK DRCQFFEAHG TGTPAGDPLE ARAIHEAFFT DGDTVPEPMY VGSVKTAIGH
LEGCAGLAGL IKALEAVKRG IIPPNQLFEN LNPALKPYVS NLRLPTESKP WPKLTPGSPR
RASVNSFGFG GTNVHAIIEQ FDNVHTQTSS SDGIISTPLV LSANSDLSLR KQIAHFAEAI
EHNDKGKIDR VIFTLTQRRS QLPLRTYFSG YDLQSLQQKL RDATAENAVL PFISQTVPPG
RPPRILGVFT GQGAQWPTMG REILKASPFA RAVIASLEES LASLAQPPAW TLTEQIMADK
ESSRLSEAAI SQPLCTAVQI MVVELLRKAG ITFNCVIGHS SGEITAAYTA GFLSASDAIR
VAYLRGVCAK LAGGENGETG SMIAVGLSYE EASAFCEENF AGLVDVAASN APTSTTLSGD
KASIDDAKAL LDAQGTFARI LKVDTAYHSH HMNPCAQPYL DKLQAARVKS LPGDESVEWY
SSVLGERITA SLHGEALCDE YWVENMVNPV LFSVASELVA EASLPCHVAL EVGPHPALKG
PFNQTYKRAT GSPLPYQGTV ARNIHDVEGL SDSLGFLWSH LGKSAVDFTA YSQAFSPSIT
AMADGLPPYA WDHTQSFWRE SRKSLNYRQR TQPPHPLLGA RSVEDTADSM RWINYLRLDD
VPWLEGHKVE GQVVYPAAGY LVMAMEAARA IDTTKGIQLI ELSDVYILSA IQLTEGSQAL
ETVFTLQVER NEPTFSTASW TLSTPMSGRN DSWKCNAKGQ LRVEFGCSDD AARLPSRNKP
IASLTSVNME RFYSALANIG LEYTGEFKQL KSIDRQLGLA TAHVSQVVPD FPAMIHPALL
DGAFQSIFAA YCWPDDGSLQ APFVPTFFRS LRIANTGHLR HGEDLVVDSF LTNTNERELT
ADMDVFQSSQ GQPVLQLQGL TCTSLLRPGP SNAKELYTKT EWEVDIASGI AQSDTQDQDT
ASDLELVDLC ERLSYFYLRE LNNAVGREEV SGFDWHYRRI FEWIDHLFPL IQSGQHATIK
TEWSSDSRDW LMQQSARFPG RIDLQLIQAV GENLPSVVRK QTTMLEHMVK DDMLNRIYKF
GLGFERANVY LGRISKQIAH RYPRMNILEI GAGTGGATKG IMESLGTTFE TYTFTDISTG
FFEAAAEAFD HWADKMIFKP LNIESDPTEQ GFPEGHYDFI IASNVLHATK SLTVTMRNTR
KLLKPGGQLL LLEVTSDIVR VKLMMSGLSG WWLGGDDGRR YGPTIPVSQW DALLKQTGFS
GVDKTVNDFV DAEKYMTSVM LSQAVDDRIE LLRQPRLTFS DWLSSQSITV VGGYFRDIGR
DILEILHQMN HGASQPVIHH VGSFEELALS NIQARSALVL EDLDEPILKD LTDDKLRGVQ
RLINESRQVL WVSKGCQRDE PFANMSIGMC RSLASEYPHI HLQHVDIEGR VSPMTASLLV
EAFLRLVYRA SLKSDDLVWS IEAELVLRED KWFIPRVKSD EALNNQLNAS KMTIHSQKTL
HGDTIEIQQR SNQFVIVDPV PCVPVSVSSP PVAITVTHSL LFPFQVGTKS SGYLCYGYTD
SQPRTRVLAI SEVNRSKVSV SPFSVWDLSS SEIDAADLLR KTALAITADR LLSDFEAGAT
VLIHESDELL GAALQWKAAE LDLNVIMTTS ESSRERSTGA MFIHALAPER LVNHIMPQHT
KAVIDLSGKD YSIVGSPLRR CLPANCKFHQ LQDILGNASQ GVADPIIHGV RDASRSSLQL
CGDGPVVKLS DLPSLRASIK DYATVVEFSA NTTIPAIVQP LEGSRLFRSD RTYLLIGCTG
GLGKALCRWM VSCGVRHLAL TTRNVAAIDQ VWLEELRIQG AQVNLYQADV SDKAALLQAY
DQIVKEMPPI CGTANAALLL SDRTFTELKV NDFTKVFGPK VKGTQNLHEL LLDQKLDFFI
MFSSLASVVG NRGQANYAAS NLFMSAIAEQ RRAKGLAASV MHIGMVLGVG YVSSTGAYEA
TLRSSNYMAI SETDLLNMFS QAILVGQPNS THAPELITGL NRFSLEPEAQ KYFWRDNMRF
CHHTLEEEHQ ERASATKVSI SQRLSEAKGT AEILAVVEEE FCTKLERLLQ AEAGFVKTSQ
SLLGLGVDSL VAAEIRSWFL KELEVDTPVL EILNTASITE LCSTVVSHLP TISGEIAPKT
EVTKQAIKTL NVVETSTAVS SALPTENEPF TIRNSPNSTQ VTSEAGVDED TSIHSKFDRA
GPLSFAQERL WFLQQFLRDH STYNVTMHYH ISGPLRLHDL EMAFQQLIHR HESLRTSFFI
DPDTDLPTQA VLKDSSFKLE QKHNSTAKIE YKAMQEMSYD LENGKVTKAV ILPDSDGEFD
LIFGFHHIAL DGYSAQIMVR DLAIAYAGQT LPSKQQDYLD FAIAQKTAKV PDTTLAYWRS
EFRELPPTLS VFDFAETKTR TPLTDYTTRA LERTISIDQG RSIKAVAKCL DATPFHIHLA
ALQVVLSDLA STKDLCIGIT DANKYDVTHI DTVGFFVNLL PLRLKISLSQ TLAEVVANAK
SKANSALSHS DIPFDVLLDE VKLPRSTTHS PLFQVILNYK MGSTQKVPLA DCQAQLVAFK
DASNPYDLTF DIETYHDGSA CISVKTQEYL YSESELSFIL DSYLQTLALF ASEPSRTIDQ
ICRPTAEQID KALTLGRGER IPSPRLETLC HYFEEFVVKQ PDDTALVTDK GQALTWCQLK
ALVNQIAMTF VEAGAKQDSR VGVYCEPSMY ILPTLLAIAE VGGVYVPLDA QNPIKRLQLM
VDDCQPDVIL IDDSTATTAR ELETNAIVIN VNTIKADPSN TFHMDIRARG NGMGYIFYTS
GTTGVPKAVA LTHTSLVHHF DGFIHYNNLS KCRMLQQAPL GFDMSLTQMT LAIMLGGTLI
VASSETRKDP MQLAQLMLAE KVTHTFMTPT LALSVIHHGY EYLRQCVNWE HASLAGEAMT
TRVTREFKRL GLRNLELLNG YGPTEITIIA TCGSNELGDT LRDTHNPSIG RALPNYSCYI
LDENMQPVRP GLAGELVIGG AGVAIGYLNR QDLTEVKFLR DPFSPAEDIA RGWTRMYRTG
DKARFLSDGR LCFLGRIAGD SQIKLRGFRI ELEDIASTIV RASDGKIPEA AVSLRGEGDS
AYLVAFVILS QFNSPSDENG YLKQLLEELS LPRYMKPARI ISIDQLPMNA SGKLDQYALD
ALPVPHEEDI VDKPLTETQE RLKLGWLKAL PFIDAAIGPD TDFFSAGGNS LRIVSLREYI
TREFGVTVSV FDLFQASTLG EMAAKIDGST TQGPTTMPID WNEETRIDAD LSIVGAQEPL
PSETANDLQV ALTGATGFLG VSILKTLLED KRVSKVHCLA VRSSSNTSDP VFSSSRVACY
PGDLSLPRLG LSQEQFDQLA KTVERIIHNG ADVSFLKTYQ SLKRSNVSSS RELARMAITR
RIPVHFVSTG GVVQLTGQDG LDEVSVADSV PPTDGSLGYV ASKWASEVIL EKYASQYNLP
VWIHRPSNIT GPNAPKADLM QNIFHYSVKT ASLPDLASWS GCFDFVPVDV VAAGIAGSIY
ETQDTVAYKH HCGREKISVE DLPSYLEAKH GKIETISVEE WLERSKAAGF DEVTAALVEK
TLSRGGIVPW LRKEAN
