AFVB_ASPFN
ID AFVB_ASPFN Reviewed; 1751 AA.
AC B8N8R0;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Non-reducing polyketide synthase afvB {ECO:0000303|PubMed:26209694};
DE Short=NRPKS {ECO:0000305};
DE EC=2.3.1.- {ECO:0000305|PubMed:26209694};
DE AltName: Full=Aflavarin synthesis protein B {ECO:0000303|PubMed:26209694};
GN Name=afvB {ECO:0000303|PubMed:26209694};
GN ORFNames=AFLA_108550 {ECO:0000312|EMBL:EED53479.1};
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 FUNCTION.
RX DOI=10.1021/np50086a008;
RA TePaske M.R., Gloer J.B., Wicklow D.T., Dowd P.F.;
RT "Aflavarin and beta-aflatrem: new anti-insectan metabolites from the
RT sclerotia of Aspergillus flavus.";
RL J. Nat. Prod. 55:1080-1086(1992).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, DOMAIN, AND TISSUE SPECIFICITY.
RX PubMed=26209694; DOI=10.1128/ec.00092-15;
RA Cary J.W., Han Z., Yin Y., Lohmar J.M., Shantappa S., Harris-Coward P.Y.,
RA Mack B., Ehrlich K.C., Wei Q., Arroyo-Manzanares N., Uka V., Vanhaecke L.,
RA Bhatnagar D., Yu J., Nierman W.C., Johns M.A., Sorensen D., Shen H.,
RA De Saeger S., Diana Di Mavungu J., Calvo A.M.;
RT "Transcriptome analysis of Aspergillus flavus reveals veA-dependent
RT regulation of secondary metabolite gene clusters, including the novel
RT aflavarin cluster.";
RL Eukaryot. Cell 14:983-997(2015).
CC -!- FUNCTION: Non-reducing polyketide synthase (NRPKS); part of the gene
CC cluster that mediates the biosynthesis of aflavarin, a bicoumarin that
CC exhibits anti-insectan activity against the fungivorous beetle
CC C.hemipterus (Ref.2, PubMed:26209694). Catalyzes the formation of the
CC aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A
CC molecules (PubMed:26209694). {ECO:0000269|PubMed:26209694,
CC ECO:0000269|Ref.2}.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000250|UniProtKB:A0A0K0MCJ4};
CC Note=Binds 1 phosphopantetheine covalently. {ECO:0000255};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:26209694}.
CC -!- TISSUE SPECIFICITY: Expressed mainly in sclerotia, with expression
CC levels 20-fold and 10-fold greater than the expression levels of this
CC gene found in mycelium and conidia, respectively (PubMed:26209694).
CC {ECO:0000269|PubMed:26209694}.
CC -!- INDUCTION: Expression is induced by the developmental and secondary
CC metabolism regulator veA (PubMed:26209694).
CC {ECO:0000269|PubMed:26209694}.
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 backbone; 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 (PubMed:26209694).
CC {ECO:0000250|UniProtKB:Q5B0D0, ECO:0000305|PubMed:26209694}.
CC -!- DISRUPTION PHENOTYPE: Impairs aflavarin biosynthesis and leads to a
CC reduction of sclerotial production (PubMed:26209694).
CC {ECO:0000269|PubMed:26209694}.
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DR EMBL; EQ963475; EED53479.1; -; Genomic_DNA.
DR RefSeq; XP_002376725.1; XM_002376684.1.
DR AlphaFoldDB; B8N8R0; -.
DR SMR; B8N8R0; -.
DR STRING; 5059.CADAFLAP00004590; -.
DR PRIDE; B8N8R0; -.
DR EnsemblFungi; EED53479; EED53479; AFLA_108550.
DR VEuPathDB; FungiDB:AFLA_108550; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_6_1_1; -.
DR OMA; IALCRLW; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; 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; -; 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; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR009081; PP-bd_ACP.
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; PF00550; PP-binding; 1.
DR Pfam; PF16073; SAT; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; SSF47336; 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; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Phosphopantetheine; Phosphoprotein; Transferase.
FT CHAIN 1..1751
FT /note="Non-reducing polyketide synthase afvB"
FT /id="PRO_0000436109"
FT DOMAIN 1670..1747
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 19..249
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000255"
FT REGION 379..755
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 910..1228
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 1291..1607
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255"
FT REGION 1610..1670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1612..1670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 554
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 1707
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1751 AA; 192912 MW; 037FC001014A7391 CRC64;
MRIFHFSNKF PPDDLADLFR RLRLHSKCPN HVILARVLEE VTDVVREEIA ELPAELRSLL
PPFQSILDLA ESFNWHQGPL SGTFECVFLV LMPVCLFVGR PDEFVFRRDT SLFTGLGLGF
LAATAIVASP SLCSVPVTVA EVVRMAMRTG LLIYQRSQDL EPQSLDGALE SWTSIVKGMG
EVAVREGIDE YNSSTDTPQP SSIYISVVEP DGSVFINGPP SRLRKFFSTS GKVQSAAHAP
LPVYGGPCHA PHLYDHSHSS WAVKKCRAKV LSRDLSHAAY LLSMADGNPL KADTVLELFE
SATYILLTSI IRWGDVVNAI TASSPLLEKD MKLQVEILRP SPVVDGLVSA IQKSHPGCSA
YVVDLGEWIF DDTHISPHGA HEKIAVIGMS CRLPGGADDL ELLWELLREG RDVHRKVPAD
RYDVDSHTDI TGKQRNTSHT PFGCFVDQPG LFDAGFFDMS PREAGQTDPT HRLALLTAYE
ALEQSGYVPD RTRSTRRERV GTIYGQCSDD YRECNAGQDI DMYFIPGNYR AFAPGRISYF
FKFSGPSFNI DTACSASLAA VQIACSVLSR GEADMVVAGG LNILTGSDSF AGLSKGFFLS
KTGNCQVFDD AADGYCRGDG IGSIILKRLS DAQQDNDNIL GLILGSATNH SSNAISITHP
HAPTQANLYR STLMQAGVRP QDVDLVEMHG TGTQAGDAAE IESVTKVFSP AVPRRSQPLR
ISSVKANVGH GEAAAGITAL IKALLIFKHN EIPPQVCLRT TLNSKFPDLR QLNVHIPKKI
IPWPRLPGRK RYIMVNNFSA AGGNTSLLLE EPPARPDPKG CPQTRFVVTV SAKSTVSLIR
NLEGLLGFLK MDPFVDLASL AYTTTARRMH HKYRIVVHGA SIQEIVKSLE QHISIAETQC
AIQKAPTIGF VFSGQGSFSQ GVGRQLFQEY PPYRNEIQRL DEICTSHGFD SILPAITSRS
SDILEISPFM AQLVTVCVQI ALCRLWRSLG VIPNVVVGAS LGEYAALYAA GTLSASDVIY
LVGQRARLMQ ELCTINSHSM LAVKATIGEI RHTVRNNAYE FACINGPRDV TLAASVEDIN
DIQQTLVSQG YRVAKLNVPF AFHSSQIEPI LEPYNKIAHS VIFRNLKTAL ISPLLSDVVF
DNKSFPPSYL RDSTRGTVQF SDAMTKAQEI GLVDSKTVWV EIGVHQTYTG AMRANIPNLE
VVAPSLRSDE SNWHTLAASM SALHSAGVHL DWNTWYKPFE SQLRLLNLPP YQWNLKNHWI
QHNGDWLLLK DKRSRTGYER SPAPAPPPLR TALVHHILEE SFGKDGGTVV IQSNVTDDEF
HAVASGHQMS GRPLVSVFAY TDIALIMARY MYSRLKSGTE LSAMDFGKVR VFQGLIPRKD
RSKPQYVRMR MQADPMCSSM PLSLHRVLDD EMNEEELAIG VVTCGDSHSW RDEWAAYSYL
LTSRIEALHQ LADQGLASRV SKDLVYTLFK NVVDYAEHYR GIQSAVMYGL EAVADVILSP
SQDSRWTAPP HHIDPITHVG GLILNAGPAM DHTNTIYIME GWESMRFSDS LMAGELYRSY
VKMNPANDNS GFFSGDVYIL HGNRVIGRVR EMTLRPLPRI LMSRFFDPPD SQYGQMAQQE
PSTALPSTPQ HTSSAKTTES TPSQQDESDN TSLATPENEN KAPISGSWPN ANSQLVRDAI
ALIASETGVE PDALTDETEF SAVGVDSLLS LVLVEKFALE LNIDLQGSFF LETPNVCDLK
AYLEGNQMTL R
