FSR1_GIBF5
ID FSR1_GIBF5 Reviewed; 2286 AA.
AC S0DTP6; G8C419;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Non-reducing polyketide synthase fsr1 {ECO:0000303|PubMed:22492438};
DE EC=2.3.1.- {ECO:0000269|PubMed:22492438};
DE AltName: Full=Fusarubin biosynthesis cluster protein 1 {ECO:0000303|PubMed:22492438};
DE AltName: Full=Pigmentless perithecia protein 1 {ECO:0000303|PubMed:23825955};
DE AltName: Full=Polyketide synthase 3 {ECO:0000303|PubMed:23825955};
GN Name=FSR1 {ECO:0000303|PubMed:22492438};
GN Synonyms=PGL1 {ECO:0000303|PubMed:23825955},
GN PKS3 {ECO:0000303|PubMed:23825955}; ORFNames=FFUJ_03984;
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, DOMAIN, DISRUPTION PHENOTYPE,
RP INDUCTION, AND PATHWAY.
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831;
RX PubMed=22492438; DOI=10.1128/aem.00823-12;
RA Studt L., Wiemann P., Kleigrewe K., Humpf H.U., Tudzynski B.;
RT "Biosynthesis of fusarubins accounts for pigmentation of Fusarium fujikuroi
RT perithecia.";
RL Appl. Environ. Microbiol. 78:4468-4480(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND FUNCTION.
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).
CC -!- FUNCTION: Non-reducing polyketide synthase; part of the gene cluster
CC that mediates the biosynthesis of fusarubins, highly pigmented
CC naphthoquinones responsible for the coloration of the fruiting bodies
CC (PubMed:22492438, PubMed:23825955). The non-reducing polyketide
CC synthase FSR1 is responsible for the condensation of seven acetyl-CoA
CC units to yield a haptaketide (PubMed:22492438). After rings A and B are
CC formed by aldol-type cyclization, the PKS-derived product is released
CC as 6-O-demethylfusarubinaldehyde (PubMed:22492438). Then, two hydroxyl
CC groups at C-5 and C-10 are incorporated by FSR3, and simultaneously
CC hydroxyl groups at C-6 and C-8 are methylated by FSR2
CC (PubMed:22492438). The aldehyde is, on the one hand, reduced by FSR3 to
CC 8-O-methylfusarubin alcohol, which equilibrates mainly with 8-O-
CC methylfusarubin and only small amounts of 8-O-methylnectriafurone
CC (PubMed:22492438). On the other hand, the aldehyde can be oxidized to
CC form 8-O-methylfusarubinic acid, a reaction driven by FSR3
CC equilibrating with 8-O-methylfusarubinlactone, finally resulting in 8-
CC O-methylanhydrofusarubinlactol after a further reduction step and loss
CC of water (PubMed:22492438). 8-O-Methylfusarubinic acid can also undergo
CC decarboxylation, resulting in 8-O-methyl-13-hydroxynorjavanicin after
CC another hydroxylation step at C-13 (PubMed:22492438). Both steps are
CC most likely also accomplished by FSR3 (PubMed:22492438). No enzymatic
CC function has been determined so far for either FSR4 and FSR5
CC (PubMed:22492438). Their deletion does not alter the product spectrum,
CC but the possibility that they catalyze specific enzymatic steps during
CC perithecium development cannot be ruled out (PubMed:22492438). FSR4
CC might possess a regulatory function in the biosynthesis of fusarubins
CC (PubMed:22492438). {ECO:0000269|PubMed:22492438,
CC ECO:0000269|PubMed:23825955}.
CC -!- PATHWAY: Polyketide biosynthesis. {ECO:0000269|PubMed:22492438}.
CC -!- INDUCTION: Expression is induced in presence of sodium nitrate, and
CC repressed by glutamine (PubMed:22492438).
CC {ECO:0000269|PubMed:22492438}.
CC -!- DOMAIN: Multidomain protein; including a starter unit:ACP transacylase
CC (SAT) that selects the starter unit; a ketosynthase (KS) that catalyzes
CC repeated decarboxylative condensation to elongate the polyketide back-
CC bone; a malonyl-CoA:ACP transacylase (MAT) that selects and transfers
CC the extender unit malonyl-CoA; a product template (PT) domain that
CC controls the immediate cyclization regioselectivity of the reactive
CC polyketide backbone; and 2 acyl-carrier protein (ACP) that serve as the
CC tethers of the growing and complete polyketide via their
CC phosphopantetheinyl arm (PubMed:22492438). At the C-terminus, FSR1
CC exhibits a reductase (R) domain instead of the canonical TE domain
CC (PubMed:22492438). In contrast to TE and TE/CLC domains, R domains show
CC sequence similarities to the short-chain dehydrogenase/reductase (SDR)
CC superfamily, exhibiting Rossman fold structure and nucleotide binding
CC motifs (PubMed:22492438). {ECO:0000305|PubMed:22492438}.
CC -!- DISRUPTION PHENOTYPE: Impairs the red pigmentation due to the
CC production of fusarubin (PubMed:22492438). Results in complete down-
CC regulation of the other five FSR genes (PubMed:22492438).
CC {ECO:0000269|PubMed:22492438}.
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DR EMBL; HE613440; CCE67070.1; -; Genomic_DNA.
DR EMBL; HF679024; CCT64762.1; -; Genomic_DNA.
DR AlphaFoldDB; S0DTP6; -.
DR SMR; S0DTP6; -.
DR STRING; 1279085.S0DTP6; -.
DR EnsemblFungi; CCT64762; CCT64762; FFUJ_03984.
DR VEuPathDB; FungiDB:FFUJ_03984; -.
DR Proteomes; UP000016800; Chromosome 2.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.1200.10; -; 2.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 2.
DR Gene3D; 3.40.47.10; -; 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; 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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR030918; PT_fungal_PKS.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF16073; SAT; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; SSF47336; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR TIGRFAMs; TIGR04532; PT_fungal_PKS; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..2286
FT /note="Non-reducing polyketide synthase fsr1"
FT /id="PRO_0000442024"
FT DOMAIN 1637..1712
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:22492438"
FT DOMAIN 1748..1823
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:22492438"
FT REGION 7..342
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22492438"
FT REGION 369..740
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22492438"
FT REGION 905..1195
FT /note="Acyl/malonyl transferases"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22492438"
FT REGION 1296..1588
FT /note="Product template (PT) domainn"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22492438"
FT REGION 1600..1639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1716..1735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1897..2145
FT /note="Reductase (R) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22492438"
FT COMPBIAS 1600..1626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 540
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 996
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 1671
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1782
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2286 AA; 250783 MW; 2371D72173AD92CA CRC64;
MASHMKLYLF GDQTFDVQPH LQHLLQKRDN LFLHEFLNQS YNALRAELFK IPYSIRKDLP
RFTCQEDLLL WDQSGPRCVA LDMAMTTLYQ LGTFISQAGI SSYDAQNSRV VGLCTGAFAA
AAVSCSSFTA DLIPMAVSSV VAAFRTGLLV TDTARRVDPS QDLNRSWALL VPGQKAAKAF
QEFWDANDGG VLTSMPYISA YAPNGITVSG PPQRLGDLAH WLASKSITSK AIPIYSAYHA
PHLYSQKDAR RIVDGLMLNK AVSPSEQIPL LSSTGSKPEE RSFATLLEDA IAQALLHPLR
WGSIFDDVQA ALETTGSQQF SVQSIGSNAE HLIYTALKKT SLRYLVPETT VPSQPTSVPS
VPDAGTSKPK LAIVAMSGRF PGAKDNEAYW DLLYKGLDVH KPVPSLRWDQ QTHVDPTGAG
KNTSATPFGC WLDDPSEFDA RFFNISPREA PQIDPAQRLA LMTAYEAIEQ AGIVPDATPS
TRPDRVGIFY GVTSNDWMET NSAQNIDTYY IPGGNRAFIP GRINYFFKFS GPSYAVDTAC
SSSLAGIHLA CNALWQGDVD TAIAGGTNVL TNPDYHAGLD RGHFLSRTGN CKTFDDGADG
YCRGEGVATI IIKRLDDAIA ENDPILGVVL GAHTNHSAES ESITRPHVGA QRVIFNKILN
EAAVDPYSVS YVEMHGTGTQ AGDATEMSSV LETFAPPVAE GKVARPESQK LYIGSAKANI
GHGEAASGVC SVIKVLQMLK KDTIVPHCGI KNKINHRFPT DLEQRNVRIA MGPTQWKKGT
EINPRRVFVN NFSAAGGNSA LLIQDAPPRK QLIASNDSRI QFPIAITAKS GVSLQGNMRS
MLKFLSTNSH VSLAELSYTT TARRIHHQHR VLIPGATSEE ICSKIETALQ NNTGVTRPKA
APKVVFTFTG QGAQYPGMGK QLFEENEFVR NELLSLDRIA QNLGFPSMLP FIQSDEPDVS
KFAPSLVQLA SVCLQITLSK LWASWGITPT AVVGHSLGEY AALNVAGVLS DTDTLFLVGG
RAQLLEQKCT RGTHAMLVVK GSQEEITEAL KGQEYETACI NSPIETVLAG PNEQIAKVKE
QLAAASFKTT LLKVPYAFHS SQLEPMVSDI EKLAGKVTFS DPKIPILCPL EGTVIENANP
FNASYLARHS RQPVNMLTAL TTAYRDGYLS DRSMVLEVGP HPAVSGMVKP TLGQQITCVA
SLQRRRAPWD MLSAALKSLY DAGASINWVD YQSNFPGAHT VVDLPAYSWD LKEYWIQYVN
DWSLRKGDPP LVINNVSKLE STTIHSVVEE SGDSEKTGIV VEADIARKDL SPLVQGHEVD
GIPLCTPSVY ADIALTLGKY LLERYQPQQK DDMVVVSDMT VSKALILRGD GSRHPIQAHA
EADWSSQSVS IKFMSFDNKG NLQEHSACVV LFKDRSHQDA LQSEALTTKQ KMQNLRNQIT
TGESARFNRP MAYRMIRPLA RFHDDYRAID EVVLNSETLE ASSKISFGTV KRDGDFHTHP
AVIDALTQSC GFAMNCNDHT DIDVDVYMNH GWGSLELFEP LDFEKEYTTY TQMHAGEDKL
WYGDVTIFDQ DRVVAFFGQI AIQGVPRRVL KVILSIESGK KGQPQRQTQD KPRNTPSQTK
DSTPKPAQNK PAAKVEPPKF STAIRIISEE SGIDVSDFTD GTTFADVGID SLLGLTISAR
FQEELDIDLD FNALFFEHPT VKDLRAFLGA DEDVSESSSS AASDSGRDTT TTGSATPELQ
EEFAESAEVE FERALEIISE ESGVARSDLD DETNFADCGV DSLLSLVIAS RFQDTFGLNI
AHEQLFMECQ TVGDLKTMLA REMGLATPAS KPAAIPAPVV SEAVAQETVV THSDTSNLAE
REQAITELVN KYTAGFKAPT SNPNGPPLGK NESVVLVTGA SGGLGSHLVY ALAQLEEVHT
VVCLNRPNRE DPTTRQYKAM RDKGIRFPEH LKSKVRIFQT DTSKPKLGVA DSEYASLIRS
VTHIIHNAWP MSAKRPLSGF ESQFQVFRNL LDLGRECASN RPADFKFSFQ MISSIGVVGQ
WGLAAGQTGK IVVPEERTTI DSLLGNGYAE AKWGCERMLD ETLHKFTDRF RPMVVRLGQI
AGSKTSGYWN PMEHFGFLIK SSQTLNALPD VDGNLNWTPV NDIADTLTDL ILSDRTPYPI
YHIDNPIGQQ WRDVNNILSD TLRIPNKVPF KEWLDMVRKA PQQDNPAALL ADFLEDTYLR
MACGGLVLDV KHSLEHSKSL SAVGPVSETV VRKYIHIWKE IGFLKTTAED KAGFEAERLR
LWGPRV
