FSDS_FUSHE
ID FSDS_FUSHE Reviewed; 4005 AA.
AC Q5SBL6;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Fusaridione A synthetase fsdS {ECO:0000303|PubMed:23614392};
DE EC=2.3.1.- {ECO:0000305|PubMed:15724180};
DE EC=6.3.2.- {ECO:0000305|PubMed:15724180};
DE AltName: Full=Fusaridione A biosynthesis protein S {ECO:0000303|PubMed:23614392};
DE AltName: Full=Hybrid PKS-NRPS synthetase fsdS {ECO:0000303|PubMed:23614392};
GN Name=fsdS {ECO:0000303|PubMed:23614392};
GN Synonyms=eqiS {ECO:0000303|PubMed:15724180};
OS Fusarium heterosporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium heterosporum species complex.
OX NCBI_TaxID=42747;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DOMAIN.
RC STRAIN=ATCC 74349 / MF6069;
RX PubMed=15724180; DOI=10.1039/b413523g;
RA Sims J.W., Fillmore J.P., Warner D.D., Schmidt E.W.;
RT "Equisetin biosynthesis in Fusarium heterosporum.";
RL Chem. Commun. (Camb.) 2:186-188(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DOMAIN, AND PATHWAY.
RC STRAIN=ATCC 74349 / MF6069;
RX PubMed=23614392; DOI=10.1021/cb400159f;
RA Kakule T.B., Sardar D., Lin Z., Schmidt E.W.;
RT "Two related pyrrolidinedione synthetase loci in Fusarium heterosporum ATCC
RT 74349 produce divergent metabolites.";
RL ACS Chem. Biol. 8:1549-1557(2013).
CC -!- FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that
CC mediates the biosynthesis of fusaridione A, a bright yellow trans-fused
CC decalin-containing tetramic acid with antimicrobial activity
CC (PubMed:23614392). The PKS module of fsdS catalyzes the formation of
CC the polyketide unit which is then conjugated to L-tyrosine by the
CC condensation domain of the fsdS NRPS module. Activity of the Dieckmann
CC cyclase domain (RED) results in release of the intermediate fusaridione
CC A (PubMed:23614392). The unstable pyrrolidinedione ring of fusaridione
CC A is opened through a reverse-Dieckmann reaction to afford its ring-
CC opened form (PubMed:23614392). {ECO:0000269|PubMed:23614392}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:23614392}.
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 (By similarity). Thus, an NRP synthetase is generally
CC composed of one or more modules and can terminate in a thioesterase
CC domain (TE) that releases the newly synthesized peptide from the enzyme
CC (By similarity). Occasionally, epimerase (E) domains (responsible for
CC l- to d-amino acid conversion) are present within the NRP synthetase
CC (By similarity). FsdS contains also a polyketide synthase module (PKS)
CC consisting of several catalytic domains including a ketoacyl synthase
CC domain (KS), an acyl transferase domain (AT), a dehydratase domain
CC (DH), a methyltransferase domain (MT), and a ketoreductase domain (KR)
CC (PubMed:15724180, PubMed:23614392). Instead of a thioesterase domain
CC (TE), fsdS finishes with a reductase-like domain (R) for peptide
CC release (PubMed:15724180, PubMed:23614392). FsdS has the following
CC architecture: KS-AT-DH-KR-PCP-C-A-T-R (PubMed:15724180,
CC PubMed:23614392). {ECO:0000250|UniProtKB:Q4WAZ9,
CC ECO:0000305|PubMed:15724180, ECO:0000305|PubMed:23614392}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000305}.
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DR EMBL; AY700570; AAV66110.2; -; Genomic_DNA.
DR SMR; Q5SBL6; -.
DR BioCyc; MetaCyc:MON-19334; -.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
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; 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; 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; 1.
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 PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 2.
PE 3: Inferred from homology;
KW Ligase; Methyltransferase; Multifunctional enzyme; Oxidoreductase;
KW Phosphopantetheine; Phosphoprotein; Repeat; Transferase.
FT CHAIN 1..4005
FT /note="Fusaridione A synthetase fsdS"
FT /id="PRO_0000441290"
FT DOMAIN 2400..2478
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 3572..3650
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 12..450
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:23614392"
FT REGION 556..880
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:23614392"
FT REGION 947..1246
FT /note="Dehydratase (DH) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:23614392"
FT REGION 1405..1589
FT /note="Methyltransferase (MT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:23614392"
FT REGION 2117..2289
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:23614392"
FT REGION 2525..2559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2579..3001
FT /note="Condensation (C) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:23614392"
FT REGION 3043..3452
FT /note="Adenylation (A) (KR) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:23614392"
FT REGION 3690..3999
FT /note="Reductase (RED) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:23614392"
FT COMPBIAS 2525..2556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2438
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3610
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 4005 AA; 440727 MW; 91EA8533FABDA2CB CRC64;
MSAPPTKQTE PIAVVGSAGR FPGGCNTPSK LWDLLRSPRD LLREIPKERF NIDAFYHPDP
LHHGTTNTRY SYFLDEDPAQ FDAQFFSITP AEAEAIDPQQ RLLLETVYES LCAAGLPIER
LRGSDTGVYI GLMCDDWSSM IQKDIDALPT YTGTGTARSI LSNRVSYFFD WQGPSMTIDT
ACSSSLVAVH EAVRLLRSGD STVAIAAGAN LILNPTQYVA ESNLRMLSPT GRSRMWDASA
DGYARGEGIA SVVLKTLSQA IADGDSIECI IRETGVNQDG RTSGLTVPSN IAQTKLIRET
YARAGLDLSK PSDRPQLFHA HGTGTKAGDP QEAQAIHNAF FSGSQSQDAV EDADELFVHS
IKTIIGHTEG TAGLASLIGT SLAIQNSTIP PNMHFKMLNP DIAPYYKHLK VPTSARPWPT
LLDGGVKRAS INSFGFGGTN AHAIIEEYVP QVNAVPILST PASAHFTPLV FSASSSASLK
TVLADQLKYL MSNPQVSLRE LSWTLAHRRS TLSYRKYISG RSYDDLCINL GEALNSEDSN
LDARSANVEE PKILGVFTGQ GAQWARMGAE LLEASPFVEK RIAELDESLA SLPESDRPEW
TIREELLADD LASRLSEAAL SQPLCTALQM ILVDLIESAG IKFAAVVGHS SGEIGAAYAA
GFISAHDAIR IAYYRGVHTK LASSPNKDVK GAMAAVGMTV EEAAGLLEEH SLSGRISIAA
FNSSSSLTLS GDEDAIDETV EILKGQSKFA RRLKVDKAYH SAHMQSCAES YLQSLQNCNM
KPLEPTGHRP QWFSSVSEDV TMTSTLCGSE YWVRNMTQPV LFSDAITSAV DNIGSFNLAI
EVGPHPALKG PAVDNLTENG VVLPYTGLLA RGKDDIEQFS SALGFVWTNL SAGSVDFGTF
DKTINGDDAT MTVMKNLPSY PFNHQYSYWA EPRSSRTYKQ LKTRPNPVLG MPNVTTTTSS
EAQWRNMLSP KEVPWMQGHK LQGQIIFPAT GYIAMAIEAV KALAGGKCLS QIRVEDLLLE
RAIAFNDDSA TTETLFSVNI DDSDHDSISA TFACYSCPDG DHSMIRNAVG RIYVKLGPSE
ASSLPFTSAE AGFNMVDVGI DRFYKELSRI GYNYAEPFKG MTSIRRRLGI ARGVLADQSG
SAWEDELVIH PGMLDTALQT LFAAFSYPGD ESLRSLHVPV SIDSIIINPY FSPVNDMKQL
HVPWETVVRD DDKSHIKADV QLFSEDSQHT FVQIEGVSLK PFTVARPEDD VTLFSHFEYL
RDSPDGESAA IGDRLGPDEL RSARDMERIA FFYLRQVSEM SVDDRAQALK HHQHLMAWAD
YTVEKCRKGD HPSVAPECLN DTQADILALT DKYRHHVDAL LIESTGQNLP ATIRAKDSIL
QHMTKDNLLG RFYEEGIGLS TANWWLAHMV KQISHRYPAM KILEIGAGTG GTTQATLPSL
GTSFSSYTYT DVSSGFFEAA EDKFKTYADR MVFKVFDMVK SPAEQGFTEG SYDMILASNV
LHVAEDLDVM MGNVRKLLKP GGFLVNLETV TNDMLRNGII MGGLPGWWIG AESGRPHGPM
LDLASWNSLL KRCGFGGIET STPVYDSIHA VAVWAAQATD DRVALLKDPL AAQPSTKADA
HLVIVGGSSL STFALLESVK SHLQDRFSSF EHLRSVESLD KTTLPPGSTV LSLADLDEPV
MKSVTQAKMD GLKTLWTQAR NILWVTKGVR YENPFSYMMF GIGRVVRFEN PNINLQLLDV
DSISDEVGSY ISEALLRHQF LDNWKKERDV VDMLWSSEPE VFLSQGTTLM PRLYQNKAQN
DRINSIRRKI VQDIDPKTTS LRLVEEGGAV DLEQVSPLEL MASIPDHANR REIAFKQTLL
QAIQVGDLGK LTLFIGADPE SPKSAVLGLT ETLTSPALVD ASCTVEIPDS AEFGRMALVT
TAAHLVADNL VHNIPKGANL MIHEADKLLR TAVSFKAKAS GITTLFTTSR SDRRSSDCTF
VHTALPTRLL KKLVKDNTCA FVDLSPPGSL SSDVGRAISK ELPSCCSYRA SRDLLGSIPR
LRPGSSLSDA RERLSKAWSD ATKATVPIDE VGSISLNDIS NHHPADEPLT VVDWTASTVR
VRIRPIDRND IFRPDRTYLL IGLSGEVGQS ICQWMVSHGA RHVVLTSRKP GVDPAFIHHL
ESLGADVRSM SLDITSRDSL MRCLDTIKRT MPPIAGVSNG ALIVADSPFT EMTLDGMNKV
LKPKVDGSML LDEVFYDEPL DFFIMFSSLT ACLGNSGQSN YAAANMFMTT LAFQRRARGV
PGSVIDLSSL MGIGHVGRSD VFNADYFRSL GATSVSEVDL HQMFAEAIHV GRPDSKESAE
IVTGMSPMLR SELEDMKVQY RMDLKFGHFC LEQSCNKGET SASSKVPVRV QLKTVKTRGE
AMRVLLDSLV ARVKKVLQIP ADEVVHETEP LIERGVDSLV ALDIRSWFMK ELDVDMPVLK
VLGGNSILDL IKDSLERLPS SVLDTSTLTE DLDIPARRQP ATKPLPEAPS AEDLYIHADN
LLPAPSTAPS LNGTSTPTST TSNDGTGSSY PASNAENDIK APTVRDSIIN SSTEVTELMS
FGQTRFWFLH HALQDSTTFN VAVSVRLEGM MELERFERAL EAVAEKHEAM RTRYFWGGEE
GDIPMQGILS KPLVRLNHKR ISDRAEAGKA LEEMRDVKWD LNDWESMKFV LLSLSDNTHW
LIFGCHHITI DGVSIQLIFA DLEMAYQGQI LTLLPDKSQY RTYSTLQRKQ FELGSFQKDI
DFYRNIIPSD VQPIPLLSFS KLTARQPQTS YKTFRADIRL DASSTAQIKQ IARHNQATNF
HLYLSVLQAL LFRLLPNTNE IFIGIADANR NDEQFLQTLG FFLNLLPIRF ERPSHKTKFG
GSIKNARNKV YAALEHSALP FDLLLSELGV SRSANSPPVF QVFVDYRQGT QERAKFASFD
AAGEEWYHPR TGYDISLDLL ENSEGDTLVT LQLQQSLYTQ EQTELFARAY VNLLKGLTKT
PGGDIPIMAP SVWADEDITK ALQVGKGPET PLSWPETVSH RIDEVVKDFG SKPALKVGTN
TALTYEDMGR RVDAIAQYMV SKGVANGDVV GIFQAPGTDW ICSMLAILRI GATYLPLDLR
NSIHRLQDSV RIAKPDMLLV DPSTLETLKS ITTGNAEVMD ISAIPHNTSV AHQVSAARGQ
DTAVILFTSG STGEPKGIRI KHSNLVAQNE GFSKQCNISP GEAFNVLQQS AFSFDFSLEQ
IFVALCNGGC LHIVPSEIRG DPFEVTRMIL EENINYTSGT PTEYEMWLRN APEHLTQCHQ
WNFAFFGGEA FSDEFVSDFR KLGLSDLKVF NNYGPSETTI ACTHQGRIDY RNSDLECPLP
AGFAAPNYAI YTVDENLNLL PINVPGEVLI GGAGVTGGYV DLDSLTQERF LPNKFIQPGS
HLANNGWNTL YRTGDRGLLR EDGGLVIRGR IDGDTQVKIR GFRVELAEIE TIILESSKGS
LKHAVVTLRE SEGAGFLAAH VVFSRHHPEA GRAEYLAGLQ AKLQVPDYMR PAIIVALDQL
PVTAHSKFDR AAVKALPLDA PLSTERDLAD GREMTPVEAK LEELWRSVLP FTPTTAITPE
SNFFHVGGSS LLLVKLHRMV KQRFSAAPKL VELMNAGKLS DMTAIIEATL STKIDWAAET
AVPDTWSEDF PMPLVKTSPQ VQGRGLNVLL TGATGYLGRH LVPALVQSAQ IEKVFCLVRH
ESDVDALRKA SEKIIIYTGD LGEVDLGLSK DEFSQLSRDS DIILHSGANR SFWDDYEVLR
PANTNSIKEL ARLALPRRIP FHFISSGSVR IYGDEEGPKI YNIDQSLPIS PTPPSDGSDG
YVASKWAAEK FLRTVASQLQ LPVTIHKPMP VPGYGPDDSH AEPESDHMVN ELVDITKRLQ
VRPTMEGLQG WADILDTQSV VNDILDSILS EQGVELQEVL HTAVRRINWQ RFIAELHSNP
ELSCLPSKDT LLWIGQAKRS GYSYLMPAHR LVVVNDDDDE MVSRR
