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Non-reducing polyketide synthase vrtA (EC 2.3.1.-) (Viridicatumtoxin synthesis protein A)

 VRTA_PENAE              Reviewed;        1824 AA.
D7PHZ2;
06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
10-AUG-2010, sequence version 1.
25-OCT-2017, entry version 35.
RecName: Full=Non-reducing polyketide synthase vrtA {ECO:0000303|PubMed:20534346};
EC=2.3.1.- {ECO:0000305|PubMed:20534346};
AltName: Full=Viridicatumtoxin synthesis protein A {ECO:0000303|PubMed:20534346};
Name=vrtA {ECO:0000303|PubMed:20534346};
Penicillium aethiopicum.
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
NCBI_TaxID=36650;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=IBT 5753;
PubMed=20534346; DOI=10.1016/j.chembiol.2010.03.015;
Chooi Y.H., Cacho R., Tang Y.;
"Identification of the viridicatumtoxin and griseofulvin gene clusters
from Penicillium aethiopicum.";
Chem. Biol. 17:483-494(2010).
[2]
BIOTECHNOLOGY.
PubMed=19168978; DOI=10.1038/ja.2008.84;
Zheng C.J., Yu H.E., Kim E.H., Kim W.G.;
"Viridicatumtoxin B, a new anti-MRSA agent from Penicillium sp.
FR11.";
J. Antibiot. 61:633-637(2008).
[3]
FUNCTION.
PubMed=24161266; DOI=10.1021/ja408966t;
Chooi Y.H., Hong Y.J., Cacho R.A., Tantillo D.J., Tang Y.;
"A cytochrome P450 serves as an unexpected terpene cyclase during
fungal meroterpenoid biosynthesis.";
J. Am. Chem. Soc. 135:16805-16808(2013).
[4]
BIOTECHNOLOGY.
PubMed=27049441; DOI=10.1038/ja.2016.35;
Inokoshi J., Nakamura Y., Komada S., Komatsu K., Umeyama H.,
Tomoda H.;
"Inhibition of bacterial undecaprenyl pyrophosphate synthase by small
fungal molecules.";
J. Antibiot. 69:798-805(2016).
-!- FUNCTION: Non-reducing polyketide synthase; part of the gene
cluster that mediates the biosynthesis of viridicatumtoxin, a
tetracycline-like fungal meroterpenoid with a unique, fused
spirobicyclic ring system (PubMed:20534346). The first step of the
pathway is the production of the malonamoyl-CoA starter unit for
the polyketide synthase vrtA (PubMed:20534346). The aldolase vrtJ
may be involved in the synthesis of the malonamate substrate for
malonamoyl-CoA synthetase vrtB (PubMed:20534346). The polyketide
synthase vrtA then may utilize the malonamoyl-CoA starter unit,
followed by sequential condensation of eight malonyl-CoA units to
form the polyketide backbone (PubMed:20534346). The cyclization of
the last ring could be mediated by the lactamase-like protein vrtG
(PubMed:20534346). The proposed post-PKS tailoring steps are an
hydroxylation at C5 catalyzed the cytochrome P450 monooxygenase
vrtE, an hydroxylation at C12a catalyzed by VrtH and/or VrtI, and
an O-methylation by the O-methyltransferase vrtF (PubMed:20534346,
PubMed:24161266). VrtC is then proposed to catalyze the transfer
of a geranyl group synthesized by vrtD to the aromatic C ring of
the tetracyclic polyketide intermediate of viridicatumtoxin to
yield previridicatumtoxin (PubMed:20534346). Finally, the
cytochrome P450 monooxygenase vrtK catalyzes the spirocyclization
of the geranyl moeity of previridicatumtoxin to afford
viridicatumtoxin (PubMed:24161266). {ECO:0000269|PubMed:20534346,
ECO:0000269|PubMed:24161266}.
-!- PATHWAY: Secondary metabolite biosynthesis; terpenoid
biosynthesis. {ECO:0000269|PubMed:20534346}.
-!- DOMAIN: Multidomain protein; including a starter unit:ACP
transacylase (SAT) that selects the starter unit; a ketosynthase
(KS) that catalyzes repeated decarboxylative condensation to
elongate the polyketide backbone; a malonyl-CoA:ACP transacylase
(MAT) that selects and transfers the extender unit malonyl-CoA; a
product template (PT) domain that controls the immediate
cyclization regioselectivity of the reactive polyketide backbone;
and an acyl-carrier protein (ACP) that serves as the tether of the
growing and completed polyketide via its phosphopantetheinyl arm
(By similarity). {ECO:0000250|UniProtKB:Q5B0D0}.
-!- DISRUPTION PHENOTYPE: Impairs the production of viridicatumtoxin
(PubMed:20534346). {ECO:0000269|PubMed:20534346}.
-!- BIOTECHNOLOGY: Viridicatumtoxin and its derivative,
viridicatumtoxin B, exhibit anti-methicillin-resistant
Staphylococcus aureus (anti-MRSA) activity (PubMed:19168978).
Moreover, viridicatumtoxin and a C2 acetyl analog, spirohexaline,
have been demonstrated to inhibit bacterial undecaprenyl
diphosphate synthase, a potential new target for antibiotic
development (PubMed:27049441). {ECO:0000269|PubMed:19168978,
ECO:0000269|PubMed:27049441}.
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EMBL; GU574477; ADI24926.1; -; Genomic_DNA.
ProteinModelPortal; D7PHZ2; -.
SMR; D7PHZ2; -.
BioCyc; MetaCyc:MONOMER-19274; -.
UniPathway; UPA00213; -.
GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
Gene3D; 1.10.1200.10; -; 1.
Gene3D; 3.30.70.250; -; 1.
Gene3D; 3.40.47.10; -; 2.
InterPro; IPR036736; ACP-like_sf.
InterPro; IPR014043; Acyl_transferase.
InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
InterPro; IPR032821; KAsynt_C_assoc.
InterPro; IPR018201; Ketoacyl_synth_AS.
InterPro; IPR014031; Ketoacyl_synth_C.
InterPro; IPR014030; Ketoacyl_synth_N.
InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
InterPro; IPR020801; PKS_acyl_transferase.
InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
InterPro; IPR020806; PKS_PP-bd.
InterPro; IPR009081; PP-bd_ACP.
InterPro; IPR030918; PT_fungal_PKS.
InterPro; IPR032088; SAT.
InterPro; IPR016039; Thiolase-like.
Pfam; PF00698; Acyl_transf_1; 1.
Pfam; PF16197; KAsynt_C_assoc; 1.
Pfam; PF00109; ketoacyl-synt; 1.
Pfam; PF02801; Ketoacyl-synt_C; 1.
Pfam; PF00550; PP-binding; 1.
Pfam; PF16073; SAT; 1.
SMART; SM00827; PKS_AT; 1.
SMART; SM00825; PKS_KS; 1.
SMART; SM00823; PKS_PP; 1.
SUPFAM; SSF47336; SSF47336; 1.
SUPFAM; SSF52151; SSF52151; 2.
SUPFAM; SSF53901; SSF53901; 1.
TIGRFAMs; TIGR04532; PT_fungal_PKS; 1.
PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PROSITE; PS50075; CARRIER; 1.
1: Evidence at protein level;
Multifunctional enzyme; Phosphopantetheine; Phosphoprotein;
Transferase.
CHAIN 1 1824 Non-reducing polyketide synthase vrtA.
/FTId=PRO_0000436828.
DOMAIN 1747 1824 Carrier. {ECO:0000255|PROSITE-
ProRule:PRU00258}.
REGION 5 400 N-terminal acylcarrier protein
transacylase domain (SAT). {ECO:0000255}.
REGION 396 771 Ketosynthase (KS) domain. {ECO:0000255}.
REGION 935 1259 Malonyl-CoA:ACP transacylase (MAT)
domain. {ECO:0000255}.
REGION 1325 1644 Product template (PT) domain.
{ECO:0000250|UniProtKB:Q5B0D0,
ECO:0000255}.
ACT_SITE 569 569 {ECO:0000255|PROSITE-ProRule:PRU10022}.
MOD_RES 1784 1784 O-(pantetheine 4'-phosphoryl)serine.
{ECO:0000255|PROSITE-ProRule:PRU00258}.
SEQUENCE 1824 AA; 199420 MW; FC9A33E0FD47BC71 CRC64;
MLHPTEVEKF PPTLLYFGNE FPNDDVNELF RRLQQHSKDR RFRLLNAYLE ESILVLQDEV
AKLPHHIKSR VPYFDNIVTL SEHGYLRDLG LGAAMESAFL LILQLGLFIG NHEAVDRELN
LPKNVTTVAG LSVGLFSAAA IALSASLAEV VRNGAECLRV SFRLGVYAGD FSSSLEAPQP
EGMLASWAHV VTGMTEESVQ SELTRVNEDL GNPETSKVFI SAADKSSVSV SGPPSRIKAA
FLQSSDLRYS KSLPLPVYDG LCHATHIYSQ DDVNTVLEIS ESLIPATRPF QLSVISSRTG
VPFTATTASD LLSEIATELV MGTIYLDNII EGIVRHIGAF PGAQSCRIDS FRTSIIFKGI
LEAIATDHPD LTIEKNDLVD WVHQDFGTRR RNDPANSKLA IVGMACRMPG GANNVEEFWQ
LLEQGRDACT TVPPDRFDLE THYDPTGKTE NAAQTPYGNF IDRPGYFDAA FFAMSPKEAE
QTDPMQRLAI VTAYEAMEMA GLVIGRTQST RRDRIGSYYG QASDDWRELN ASQNIGTYAV
PGGVRGFTVG RINYFFKLSG PCLCIDTACS SSMAAVHAAC TALWAGDVDV ALAGGVNIIT
DPDNYAGLGN AHFLSPTGQC KVWDKGADGY CRAEGIGSVV IKRLEDAEAD NDNILAVVLS
AATNHCADAI SITHPHAGHQ KDNCRRVLRK AGVSPMQVSY VEMHGTGTQA GDAIESESVL
DVFAPLKPLR RPDQRLHLGA VKSNIGHGEA AAGISSLIKM LLMFQKNAIP PHIGIRTEMN
PQLPKDLGRR NAGLVFETTP WLRPEGKKRI SVVNSFGAHG GNTTLLLEDA PERHRQRISP
ESTDGRSVYA ISVSAKSKKS LQGNLSSLLG YLEQHPDTDL ADLSYTTCAR RTHHNLRVAT
VVSSVSALQK FLRSAIDSNI ATTVQSVPSN IPSVVFTFTG QGASDRGVRQ ELFDDFPAFR
TQVLQLDQLV QRLGFPSVVP ALRGSTDEEV LSPVVSQLSI VVLEIALSRF WRLLGIRPSA
VIGHSLGEYA ALEVAGVLSA ADVLYLVGRR AQITEQRCTP YGHSMLSVLA TPDEIDRVVR
RVPETSNVEY EVSCQNTHED TVLGGAKADI EAIRKVLETT SYKCVPLAIP FAYHTSQMDV
VVDELEEIAK NIPFKAPSIP VLSTMLGTVV FDGKTINPTY LRRQTRGTVK FVAAVETARD
LGLIDEKTVW VDLGPHPVCV GFIRKLSPES RIAASCRRNE ENLSTITKSL VTLHLAGATP
LWNEFFRPNE QVYRLLNLPK YSWNETNYWI PYLGTWALDK ALLKYGITPV GAKAPATLPA
AGLRTSTIHQ TTLETIDSMT ATLHVLSDMQ APEFRAAVYG HTMNNCGVAT SSIWTDMALA
VGEYLYRKLV PQAKEVHMNV CDLEVLHAQV ISKVKGCSQP LALEAHLDLD MQYMSLKWYN
TNAATGERAP EWFASAAVRF ENPDAWTAEW NRTGHLVLGR IETLRRLAAD GVANRISKRL
AYTLFKNVVD YSDWYRGIDD VIMNDYEAVA NVTLIPDRHG TWHTPPHWID SVCHLAGLIM
NGSDASNTQD FFYVTPGSDS FRLLKPLAPG AKYISYVRMF PLSAEAGNMY AGDVYILKDD
VIVGVLCQIR FRRVPRLLMD RFFSPPTADN AGVHGTPGSQ RSQAPPAATH AATKSPQKTL
QVPSGHVPNK ASIVDTNHVQ ASHPSAVPVR HDQSNGVSGV SDSDSSTSIT SSNSTADTST
TPTESEDADS GLVGQCIKII SRETNLDMSE LTPDATFAQL GVDSLMSLVL SEKFRNELGI
DVKSSLFLEC PTIGEVKEWI DQNC


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