FLUP_ASPFN
ID FLUP_ASPFN Reviewed; 1120 AA.
AC B8NYX0;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Cluster 41 polyketide synthase {ECO:0000303|PubMed:27647242};
DE EC=2.3.1.- {ECO:0000305|PubMed:27647242};
GN Name=fluP {ECO:0000303|PubMed:27647242}; ORFNames=AFLA_114820;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
RN [2]
RP IDENTIFICATION OF THE GENE CLUSTER 41.
RX PubMed=20447271; DOI=10.1111/j.1364-3703.2009.00594.x;
RA Georgianna D.R., Fedorova N.D., Burroughs J.L., Dolezal A.L., Bok J.W.,
RA Horowitz-Brown S., Woloshuk C.P., Yu J., Keller N.P., Payne G.A.;
RT "Beyond aflatoxin: four distinct expression patterns and functional roles
RT associated with Aspergillus flavus secondary metabolism gene clusters.";
RL Mol. Plant Pathol. 11:213-226(2010).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=27647242; DOI=10.1016/j.funbio.2016.07.010;
RA Chang P.K., Scharfenstein L.L., Ehrlich K.C., Diana Di Mavungu J.;
RT "The Aspergillus flavus fluP-associated metabolite promotes sclerotial
RT production.";
RL Fungal Biol. 120:1258-1268(2016).
CC -!- FUNCTION: Polyketide synthase; part of the gene cluster 41 that
CC mediates the biosynthesis of an extracellular and diffusible metabolite
CC that is able to stimulate colony sclerotial production
CC (PubMed:27647242). {ECO:0000269|PubMed:27647242}.
CC -!- INDUCTION: Expression is positively regulated by developmental
CC regulators veA and velB but not by the global regulator of secondary
CC metabolism laeA (PubMed:27647242). {ECO:0000269|PubMed:27647242}.
CC -!- DISRUPTION PHENOTYPE: Reduces the production of sclerotia
CC (PubMed:27647242). {ECO:0000269|PubMed:27647242}.
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DR EMBL; EQ963487; EED44780.1; -; Genomic_DNA.
DR RefSeq; XP_002385535.1; XM_002385494.1.
DR AlphaFoldDB; B8NYX0; -.
DR SMR; B8NYX0; -.
DR STRING; 5059.CADAFLAP00013400; -.
DR EnsemblFungi; EED44780; EED44780; AFLA_114820.
DR VEuPathDB; FungiDB:AFLA_114820; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_16_6_1; -.
DR OMA; FDAGYWA; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
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:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.40.366.10; -; 1.
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; 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; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 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; PF00550; PP-binding; 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; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 2: Evidence at transcript level;
KW Multifunctional enzyme; Oxidoreductase; Phosphopantetheine; Phosphoprotein;
KW Transferase.
FT CHAIN 1..1120
FT /note="Cluster 41 polyketide synthase"
FT /id="PRO_0000438551"
FT DOMAIN 1042..1116
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 10..433
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 539..796
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 804..943
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000255"
FT ACT_SITE 178
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 625
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 1076
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1120 AA; 120561 MW; 934D88B2C1201DAA CRC64;
MEANDSPHDV AVVGMGCRLP GNNNTPEELW RSILQKVDAS SEIPRMRWEP YQQNAQNARS
IGKVPRRGYF VKNLENFDAG FFNISPKEAE QMDPQQRLVL EVTWEALENA GIPLSSLSGS
DAAVFMGVNS DDYGKLLLED LPHVEPWMGI GTAYCGVANR ISYHLNLMGP STAVDAACAS
SLVAIHLGRQ AILSGESKVA IVGGVNAIFG PGLTSVLDKA GALSSDGRCH SFDDAASGYG
RGEGAAVVIL KNMAEAVKDG DHILATLKGT AVAQDGRTNG IMAPNQKAQE LVARKALDVA
RVDASTIDYV EAHATSTPVG DPTEVSAISA VYGKGRSPDK PCYIGSVKPN VGHLEAGAGA
VGFIKAVMSV QKGILPPQAN LKTLNTRVNW SEGVQVVQDI EDWPSSGYPR RAGVCSYGYG
GTVSHAIIEK YIQTGPAIYS KEQWPKGTQV LLLSSPQRRS LETQAATQAE WMSTVGKQND
LRCVAATLGT RRSHHKYRAA FVVESHDDAA EKLNAFACQT PTKWTTSGGK PEGDDRPVVW
VFSGHGAQWT DMAKDLLQYR VFRDVIESVD ILVQKEMGFS AIQAMEMGVL NGSDQVQVLT
YLMQIGLSEV LRSLGVSCGA VIGHSVGEIA ASVAAGCITP AEGTLIVTRR AKLYRRFMGA
GGMALVCAPL EQITIEISTQ NVNNLVVAIN SSPSSCVVSG PKEEIEAFAL NLNNKGIKTI
HVDTDIAFHH PMLGELMEPL AEALVGYVSP SQSKVAIYST SASDPRSTMD RGIRYWLDNM
VNPVQLTSAI SAAAEDASPL APIIKKILSM ESRGATIQAI AIDISSHDAA SQLSSRIDDL
CFPPIRGVVH AAGVLHNEHV LSVTPDSFER VLAPKIAGSL TLNMLFPPKT VDFMVLFSSC
GQFFGFPGQA SYASGNAFLD ALATYRRSQG DNTIAMQWTS WREIGMAAGS EFVRAELATK
GITDISQEEA FQAWMHVSKY DVDHAVVLRS RALEKHEPLP SPLLVDIAIH KISSILTPPP
TPPLSASSDL LPLPRNPADR FDSLSRQVRE CVANVLQMET DEVASQEPLS NMGMDSVMTV
HLRGRLQKSL GVLVPPNLTW SHPSIDHIVK WLMEKTNDKE
