BIK1_GIBF5
ID BIK1_GIBF5 Reviewed; 2036 AA.
AC S0DZM7;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=Bikaverin polyketide synthase bik1 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:17696354, ECO:0000269|PubMed:19400779};
DE AltName: Full=Bikaverin biosynthesis protein 1 {ECO:0000303|PubMed:19400779};
GN Name=bik1 {ECO:0000303|PubMed:19400779};
GN Synonyms=pks4 {ECO:0000303|PubMed:12409099}; ORFNames=FFUJ_06742;
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 [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 [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=12409099; DOI=10.1016/s1087-1845(02)00501-7;
RA Linnemannstoens P., Schulte J., del Mar Prado M., Proctor R.H., Avalos J.,
RA Tudzynski B.;
RT "The polyketide synthase gene pks4 from Gibberella fujikuroi encodes a key
RT enzyme in the biosynthesis of the red pigment bikaverin.";
RL Fungal Genet. Biol. 37:134-148(2002).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17696354; DOI=10.1021/ja074865p;
RA Ma S.M., Zhan J., Watanabe K., Xie X., Zhang W., Wang C.C., Tang Y.;
RT "Enzymatic synthesis of aromatic polyketides using PKS4 from Gibberella
RT fujikuroi.";
RL J. Am. Chem. Soc. 129:10642-10643(2007).
RN [4]
RP FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RX PubMed=19400779; DOI=10.1111/j.1365-2958.2009.06695.x;
RA Wiemann P., Willmann A., Straeten M., Kleigrewe K., Beyer M., Humpf H.U.,
RA Tudzynski B.;
RT "Biosynthesis of the red pigment bikaverin in Fusarium fujikuroi: genes,
RT their function and regulation.";
RL Mol. Microbiol. 72:931-946(2009).
RN [5]
RP INDUCTION.
RX PubMed=19838698; DOI=10.1007/s00253-009-2282-3;
RA Rodriguez-Ortiz R., Mehta B.J., Avalos J., Limon M.C.;
RT "Stimulation of bikaverin production by sucrose and by salt starvation in
RT Fusarium fujikuroi.";
RL Appl. Microbiol. Biotechnol. 85:1991-2000(2010).
RN [6]
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 [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26382642; DOI=10.1016/j.fgb.2015.09.006;
RA Arndt B., Studt L., Wiemann P., Osmanov H., Kleigrewe K., Koehler J.,
RA Krug I., Tudzynski B., Humpf H.U.;
RT "Genetic engineering, high resolution mass spectrometry and nuclear
RT magnetic resonance spectroscopy elucidate the bikaverin biosynthetic
RT pathway in Fusarium fujikuroi.";
RL Fungal Genet. Biol. 84:26-36(2015).
CC -!- FUNCTION: Polyketide synthase; part of the gene cluster that mediates
CC the biosynthesis of bikaverin, a red pigment also considered as a
CC mycotoxin (PubMed:12409099, PubMed:17696354, PubMed:19400779). The
CC first stage is catalyzed by the polyketide synthase bik1, which
CC catalyzes the formation of the intermediate SMA76a also knowm as pre-
CC bikaverin (PubMed:12409099, PubMed:17696354, PubMed:19400779). FAD-
CC dependent monooxygenase bik2 might then be responsible for the
CC oxidation of pre-bikaverin to oxo-pre-bikaverin which is in turn
CC methylated by the O-methyltransferase bik3 to me-oxo-pre-bikaverin
CC (PubMed:26382642). A further cycle of oxydation and methylation by bik2
CC and bik3 leads to the final product of bikaverin, via a nor-bikaverin
CC intermediate (PubMed:19400779, PubMed:26382642).
CC {ECO:0000269|PubMed:12409099, ECO:0000269|PubMed:17696354,
CC ECO:0000269|PubMed:19400779, ECO:0000269|PubMed:26382642}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:12409099, ECO:0000269|PubMed:17696354,
CC ECO:0000269|PubMed:19400779, ECO:0000269|PubMed:26382642}.
CC -!- INDUCTION: Expression is repressed during the growth phase, but is
CC induced as the growth rate decreases due to nitrogen depletion of the
CC culture medium (PubMed:12409099). Highly expressed only under acidic
CC culture conditions (PubMed:12409099, PubMed:19400779). Also induced by
CC salt starvation (PubMed:19838698). Expression is repressed by
CC regulatory gene, areA, a transcriptional regulator responsible for the
CC activation of nitrogen assimilation genes (PubMed:12409099). Expression
CC is also negatively regulated by vel1 (PubMed:20572938).
CC {ECO:0000269|PubMed:12409099, ECO:0000269|PubMed:19400779,
CC ECO:0000269|PubMed:19838698, ECO:0000269|PubMed:20572938}.
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
CC back- bone; a malonyl-CoA:ACP transacylase (MAT) that selects and
CC transfers the extender unit malonyl-CoA; a product template (PT) domain
CC that controls the immediate cyclization regioselectivity of the
CC reactive polyketide backbone; and an acyl-carrier protein (ACP) that
CC serves as the tether of the growing and completed polyketide via its
CC phosphopantetheinyl arm (By similarity).
CC {ECO:0000250|UniProtKB:Q5B0D0}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of bikaverin and its
CC intermediate oxo-pre-bikaverin (PubMed:12409099, PubMed:19400779,
CC PubMed:26382642). {ECO:0000269|PubMed:12409099,
CC ECO:0000269|PubMed:19400779, ECO:0000269|PubMed:26382642}.
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DR EMBL; HF679027; CCT67991.1; -; Genomic_DNA.
DR AlphaFoldDB; S0DZM7; -.
DR SMR; S0DZM7; -.
DR STRING; 1279085.S0DZM7; -.
DR EnsemblFungi; CCT67991; CCT67991; FFUJ_06742.
DR VEuPathDB; FungiDB:FFUJ_06742; -.
DR HOGENOM; CLU_000022_6_0_1; -.
DR Proteomes; UP000016800; Chromosome 5.
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; -; 1.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 2.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
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; 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; 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; IPR001031; Thioesterase.
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; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF16073; SAT; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53474; SSF53474; 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; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..2036
FT /note="Bikaverin polyketide synthase bik1"
FT /id="PRO_0000436338"
FT DOMAIN 1653..1730
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 8..242
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000255"
FT REGION 370..742
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 908..1209
FT /note="Acyl/malonyl transferases"
FT /evidence="ECO:0000255"
FT REGION 1295..1599
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255"
FT REGION 1628..1654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1733..1758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1629..1654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1733..1753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 541
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 997
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 1857
FT /note="For thioesterase activity"
FT /evidence="ECO:0000250|UniProtKB:Q03149"
FT MOD_RES 1690
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2036 AA; 221460 MW; FCA97D2EB05774D4 CRC64;
MASSADVYVF GDQSTPVLDK LQALVRVKDN ALLTSFLGEA FLAVRREIVS LSSLERKSIP
EAESLSLLLE GVRRSEPHAA LDSAFVCIYE IGYYIDYLAR SDKQHPPAAP SLLLGICTGS
IAAAAVSCAK DVFEISRLGV EAATVAFRLG MHVRRRAENL GYSTPSSWSM ILSSNQEELV
SEALKEFSKE KNLTYSSRPY ISATGPGFTT ISGPPSILES VKSCDTFSGK RLYPAPIYGP
YHNSSSYSES SLEHGLASIL EDVGFLENEM LIPIISCASG SRLDQLSFGN LLKNVLSSAL
SQQIRMDLVT DALVETVSGT EATLIPVNAQ TTVCSLADWL AKRGATTRIG PTLESLTKDR
AEPNLAPGDE NKIAIIGFSG RFPEADNLDE FWDLLIRGLD VHKPVPEERF ARDHYDPTGQ
RKNTSQVQYG CWLKSAGYFD TQFFHMSPKE AMQTDPAQRL ALLTAYEALE MAGVVPDRTP
STQRNRVGVY YGTTSNDWGE VNSSQDVDTY YIPGANRAFI PGRVNYFFKF TGPSIAVDTA
CSSSLAAINL AITSLKNRDC DTAIAGGTNV MTNPDNFAGL DRGHFLSRTG NCKAFDDGAD
GYCRADGIGT LILKRLPDAI ADSDPIFGVI LGAHTNHSAE SVSITRPLAD AQEYLFKKLL
NETGIHPHDV SYVEMHGTGT QAGDAVEMRS VLNSFAFDHS RPRDKSLYLG SVKANVGHAE
SASGVLAIIK VLLMMQKNTI PPHCGIKTKI NQGFPKDLDH RGVRIALKDS VDWSRPEGGK
RRVLVNNFSA AGGNTSLLLE DGPAVHPARQ HQDGDARTEH VVAVSARSTK ALEENLKALE
AYIANSWAPE GELLSQLSYT TTARRVHHSR RVAFVTNGLD DLRKSLLKAA TDAGQVKGIP
AVSPKVGFLF TGQGAQETAM AIGYYKSFSS FRSDIHQLDS IATLQGLPSV LPLIHGTTPV
EDLSAVVVQL GTCIIQISLA RFWISLGITP QYVIGHSLGE YAALQIAGVL SVNDAIFLCG
HRAALLDKKC TAYTHGMVAV KAAADDLRQH ISSDLKVEIA CVNGAEDTVL SGPNADIESL
CGKLTQAGYK LHKLEIPFAF HSSQVDPILD DLEELASQVG FHEPKLPIVS PLLRTLLTGD
TLGPQYIRRH CRETVDFLGA IKMAESQGIM DRSGMCIEIG AHPILTRMVK SIIGQDFRCL
ASLRRKEDHF KTLADSLCAL HLAGFSVNWD EYHRDFASSR NVLQLPKYSW QLANYWMQYK
YSWCLTKGDA PVENGPVGAV VQARALRLSD SVHNVIEQVH GDKRSSITVE SDMHDPSLLA
IAQNHRVNGL TMAPSTLFAD IAFTLAKHLI QNHGLDTHTN LPSINNMAVE KALIVGETGP
QLFRASLDMD WTTMRGSVRI FSVGANGKQT TLHAVCDVAV ENPSSHRESW QSNAYLIQRG
IKQLVQGASD GSAHMMRRGL LYKIFSNSVQ YGSAFQGIEQ VWFDSEGLEG TGKVFMPSGK
DTFALNPYCC DSLGHITGFI MNCSDSLDLD DHVYINHGWR TLRLVEPYQC DVQYQTYVKM
QAVGSDDSTY SGDVHVLRDG KIIGICGGVT FKKVARKVLE MLLPKPSGAK AKHGVVKHVA
PEPVKHVVLT PPSTTSHSVG TTSPPEPTES PVGSASGLIQ KALEIIADEI GVDISQLTDT
TLLADLGVDS LMSLTILGNF REELDLDIPA AQFYEFSTVQ DLKSFLGAND QDFSSSNSEA
ESSASSAAST SPSDHGDDVV EEVKPVVAEI PRSTSTILQG TKHCSQTLFL FPDGAGSATS
YVTLPSISSD MRVIGLNSPY LTKPHEFNCA LQDITGSYLN EVRRRQPQGP YHLAGWSAGG
VSAFDAARQL VSEGEVVESL ILIDSPNPVG LGKLPKRMYD FLEKSGIFGA FEMGEEAQAP
PDWLFQHFCV FIEALDRYVP EPFEHGMAPK TTIIWAADGV CKNPDDPRPE AQPDDPRGMN
WLLNNREDFG PNGWDEFIGA GNISTMAIEN ANHFTMMREP IASALCAKIR ETMGVN
