PYVA_ASPV1
ID PYVA_ASPV1 Reviewed; 3814 AA.
AC A0A2V5GX43; A0A7M4B2X1;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 1.
DT 25-MAY-2022, entry version 20.
DE RecName: Full=Hybrid PKS-NRPS synthetase pyvA {ECO:0000303|PubMed:33117309};
DE EC=2.3.1.- {ECO:0000269|PubMed:33117309};
DE EC=6.3.2.- {ECO:0000269|PubMed:33117309};
DE AltName: Full=Pyranoviolin A biosynthesis cluster protein A {ECO:0000303|PubMed:33117309};
GN Name=pyvA {ECO:0000303|PubMed:33117309}; ORFNames=BO99DRAFT_417425;
OS Aspergillus violaceofuscus (strain CBS 115571).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450538;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DOMAIN, FUNCTION, DISRUPTION PHENOTYPE,
RP AND PATHWAY.
RX PubMed=33117309; DOI=10.3389/fmicb.2020.562063;
RA Wei X., Chen L., Tang J.W., Matsuda Y.;
RT "Discovery of pyranoviolin A and its biosynthetic gene cluster in
RT Aspergillus violaceofuscus.";
RL Front. Microbiol. 11:562063-562063(2020).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115571;
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that
CC mediates the biosynthesis of pyranoviolin A, a pyranonigrin analog with
CC a C-3 methoxy group (PubMed:33117309). Initially, the PKS portion of
CC pyvA synthesizes C-10 carbon chain from 5 molecules of malonyl-CoA,
CC which is then condensed with the thiolation (T) domain-bound glycine
CC activated by the adenylation (A) domain (PubMed:33117309). The
CC subsequent chain release by Dieckmann condensation (DKC) could be
CC catalyzed by the TE domain present at the C-terminus of pyvA and/or the
CC alpha/beta hydrolase pyvD, installing the tetramic acid moiety
CC (Probable). The FAD-dependent monooxygenase pyvC next epoxidizes one of
CC the olefins of the polyketide part, and the epoxide ring-opening
CC induces the dihydro-gamma-pyrone ring formation (Probable). The
CC cytochrome P450 monooxygeanse pyvB would be responsible for the 2
CC consecutive reactions, in which the dihydro-gamma-pyrone is oxidized to
CC gamma-pyrone and C-7 is hydroxylated to yield pyranonigrin F
CC (Probable). Finally, the O-methyltransferase pyvH methylates the C-3
CC hydroxy group to complete the biosynthesis (Probable).
CC {ECO:0000269|PubMed:33117309, ECO:0000305|PubMed:33117309}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:33117309}.
CC -!- DOMAIN: The N-terminal part acts as a polyketide synthase and includes
CC a ketosynthase (KS) domain that catalyzes repeated decarboxylative
CC condensation to elongate the polyketide backbone; a malonyl-CoA:ACP
CC transacylase (MAT) domain that selects and transfers the extender unit
CC malonyl-CoA; a dehydratase (DH) domain that reduces hydroxyl groups to
CC enoyl groups; an enoylreductase (ER) domain that reduces enoyl groups
CC to alkyl group; a ketoreductase (KR) domain that catalyzes beta-
CC ketoreduction steps; and an acyl-carrier protein (ACP) that serves as
CC the tether of the growing and completed polyketide via its
CC phosphopantetheinyl arm. {ECO:0000305|PubMed:33117309}.
CC -!- DOMAIN: The C-terminal part acts as an NRP synthetase composed of
CC discrete domains (adenylation (A), thiolation (T) or peptidyl carrier
CC protein (PCP) and condensation (C) domains) which when grouped together
CC are referred to as a single module. Each module is responsible for the
CC recognition (via the A domain) and incorporation of a single amino acid
CC into the growing peptide product. PynA contains one module and
CC terminates in a thioesterase domain (TE) that releases the newly
CC synthesized peptide from the enzyme. {ECO:0000305|PubMed:33117309}.
CC -!- DISRUPTION PHENOTYPE: Completely abolished the production of
CC pyranoviolin A. {ECO:0000269|PubMed:33117309}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=FAA01291.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BR001648; FAA01291.1; ALT_INIT; Genomic_DNA.
DR EMBL; KZ825234; PYI13694.1; -; Genomic_DNA.
DR SMR; A0A2V5GX43; -.
DR Proteomes; UP000249829; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; -; 2.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 3.40.366.10; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
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; IPR013149; ADH-like_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR011032; GroES-like_sf.
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; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020843; PKS_ER.
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; PF00107; ADH_zinc_N; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 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; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; SSF47336; 2.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 4.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 2.
PE 3: Inferred from homology;
KW Acyltransferase; Ligase; Multifunctional enzyme; NADP; Phosphopantetheine;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..3814
FT /note="Hybrid PKS-NRPS synthetase pyvA"
FT /id="PRO_0000452816"
FT DOMAIN 2141..2220
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 3304..3379
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 1..343
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:33117309"
FT REGION 441..758
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:33117309"
FT REGION 835..1149
FT /note="Dehydrogenase (DH) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:33117309"
FT REGION 970..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1520..1836
FT /note="Enoyl reductase (ER) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:33117309"
FT REGION 1864..2036
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:33117309"
FT REGION 2228..2270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2273..2718
FT /note="Condensation (C) domain 7"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:33117309"
FT REGION 2738..3149
FT /note="Adenylation (A) domain 8"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:33117309"
FT REGION 3257..3304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3428..3680
FT /note="Thioesterase (TE) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:33117309"
FT COMPBIAS 2228..2266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 87
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 533
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 867
FT /note="For beta-hydroxyacyl dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2180
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3339
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 3814 AA; 416918 MW; F3D8FC833A48F152 CRC64;
MDPQQRLLLE VVFEAFEDAG ISLEEMNGSR TSVLCGAFTN DYNAMLTKDL EYYPKYTVTG
TGNAILANRI SYAFNLKGMS LTIDTACSSS LVGFHLGAQA ILNGDCEMAI IVGSALHFDP
NIFITMTDLG MLSQEGRCRA FDAGGKGYAR GEGICAVILR GQMQAEMHGD HIRALVRATG
SNHDGMTQGI TLPSSEAQEA LIRRTYQSCG LDPADTQYVE AHGTGTARGD PLEMRAIGAC
FSSPRRSDPL YVGSVKSNIG HAEGASGLAG LIKASMALEK GQIPPNMHFK HPNPEIAFAD
WQIEVPTRVI DFPSNAQGTR RVSINSFGYG GSNAHVILES YDQLPHVQPT DPGAHRPYLV
PLTSHTEKAG KLMVEKLGAY LDDRPSTLVV DLAHSLATRR TLHDERSFAV GASAADIRTQ
LSEGLPAWTK VRREPVRLGF VFTGQGAQWH AMGRQLLEQC PFFRHTLERA DRILATLPDK
PEWSIVTELT QPKETSRLGE TRLSQPICTA LQLAILDLLK SWGIVPQATV GHSSGEVAGA
YAAGILTFEN AMYAAYYRGL HMSSPRSSTS PGRDAIPGAM LAVGLGEAEA MAETESYRGR
AVVAAVNSPS SVTLSGDADA IAEIKERLDA QKVFARRLQV QQAFHSHHMD PLAPAYEEAL
RNCPGFAATA PACRFFSSVT ARVANPDTMG PQYWSANMTG TVRFSDALIG VLLDDLEDPN
VDALVEIGPH PALKGPARQV MKSVNMDLPY FASLSRGVPD YEGILALAGQ LFQLGYPVDL
TAVNSDTYLA DSDPPRQTHR AQRIPDLPLY AWDHSDRYWA ETRLIKEHRL RPHHHPILGA
KMPGSIEGHV RWRNYLRTRE LPWLVDHMVD NKVTFPAAGY VTLAIEAALR MKDTVMAAQG
VSLRNLSIKS ALVLDESEMG SEVVVDIRPQ TTSAKSRSDT WLEFTIFSYN GSLTCAEHCT
GLISISTATT ADGAPSRKPY RQHPQPQPGR MSTASFPAQS FYTHLRQLGL QYGEHFQLLT
GTIESGAGFS SSMLTFEPAQ YAAQPADRTV VHPTMLDAAF HTIFAALEGL SGRTLQTAFV
PTFVHSLDIF PAMLSGMDAP RPLEARVASS AHFSGPRAAV SDVDMYRQGD GEALLSLAGL
RLTSLSNGRA AHNRSLFFRT RWQPAFDQLA EDSPALQDQT LAGVLDLFLH QHPDTKILHF
TPDINQTRQL VGCLVDQGSE RRRFRSITPV ATGGAFAEEL ERVQREQPGC LVTGEPEPEA
YDLVIVSEAQ EAHPLPFLRD GGYVISHGSA IDETNLTKRF QCADVEVWQR TRETRRDVRP
LLLAMAPTPS RRTLDLASHI RAANPDRPVS CLGLQELLAR MTGVEDVVVL ASLDRDLLSG
LDPQGELFFE ATRALLIRPD VNVLWLLQDT TAPRHVDSLG SSMIVGLART ARSENPSSRI
VTLDLPVDWS PAAVVPWLPQ LLDPEVHEDE FHLRDQVLSI PRIENDDGLN SKVPGGVSSG
PRPESFSAQR PMRLAIGQAG LLETLVWEDD VEILNEPLPD DEIEIEVKAS ALNFRDVAAA
MGIIDDHRLG DECAGLVRRV GQQVDPAAFQ PGDRVVALRP GRGAHRSVVR NPACHCFRLG
PMPFEQATAL PLILTTAYYS LVETARLQPG ETVLIHCAAG GVGQMAIQIA QQIGARIIAT
VGSPAKRDLL QSRYGLTEAH ILSSRDASFV DGVMQLTGGR GVDVVLNSLS GKLLHASWNS
LATFGRFIEI GKRDIHENTL IEMDPFRRNV LFASVDMVTI YAQNRALGAR IFDHCCNMVH
EGRIQLPATI LALPYSEAVQ GFRLLQMGRH TGKVVLVAED QGDQVPVSPP TWNAVANRLS
PDKTYLLVGG LGGLGRTLTE WLVQRQAKRI AFLSRSGADR PEAQATVAWL RARGIAVSVH
AADVADPGHV QACIKAIPDL GGVFHAAMVL ADAPLERMSY AQWHRCVQPK VRGAYNLHCA
TVHCPLDFFV CFSSISAFFG SKAQANYAAA NVYLDSLVRY RRQLGLPASS MNCGRITGVG
VAAADASLER FMVEEGFDGV NRQELLYQIE EAIFSADHPA PLSGRGTDMS QTLTGVTLER
DDVYWAQRSI FRNLYRNHDV EGQSRPGADE VNLSVQLART IDLSDRVALL MERFVDKVSV
VLGLSPESLK PADPVYGLDS LVAVELRNWF TKSVGVDIAL FDVLGSPSIQ ALVEKAIGLF
DAQVQQQQQQ QQSVQSSSAP SNDDQSPTFN KNLDSQDPST SLQIPKADCS RPLPMSTFQN
RLWVSHRFAA DKSRINLAIT MHLRGQADHG ILEQALSELI ARNPILRTAY GEGEAQDEQR
VMAPRPFHLG FHDLSKSGPS EGPTASLETL VGSLKRKEMR IEEGEVLEAT LVQRSSTECA
LVLIMHHICT DRSNSQSFVR QLAALYDALR QGRSLSTIPA PKVTYADFTL WHNQLLTSPS
MGKGVEYWKQ TLAGMPASCQ LLPFAKGERP SWDEYGRETV VAALSARQLQ RMKRICSQAR
TSPFHFLLAA FRAFLHRYTA DEDLTILMVD GNRPHADLGE VLGFFVNMAP IRCRDACAGS
FETLLKTIGG RVLEAMAHSH VPFDVIVAQT QGARTPAHFP VSQVLVNYQQ PDEQARYQTT
DFTFQGTEVQ NMPTGCELSL QAREDAEHGL QLELEYATAL YEDGDMRCFF DNFQTFVTSL
IQDHRQSIPE VRLAGTLELE RLALHCWNSH PPDHGWQPLN LPRRIVEVAE TQPRAIAITT
SAGEAVTYQD LVASARRVAF SLQNLGIGPG QVVGILASPG IELVTAMLGA LFNRCGYVPL
DPTMAVGRLA YIVGDSGMQL LLVDEESDPL ASSLGRESPS LPNVMSIKNA TRAAWPADLP
RSLPTDPFYM MYTSGSTGTP KGVPLTQENV GEMLAAMQAR FNFTREDRFL HQISPSFDLS
VVELFSPLCV GAKLCIATKT TRSDPRLLGD YLRQASVTVT YFTPTQFALV LEHSGASLVA
CPDYRIALLC GERLPTRLAE AFHQLACAAT LYNAWGPTEA AVQTTIHRVQ WPADQTLNIP
IGHAVGSCRH YIVDAAMNPL PVGFVGEICI GGPQVARGYW NRAESNRQQF LRNPFASPDD
HRRGWTRLFR TGDLGRFLPD GQLEFLGRIA GDKQIKLRGF RIDLGEIEHV LHRHSGTPDG
QGIVDLAVIA QSAPEDADAL TDDRWLVAFI VPKQAIPTEA AKRAYATLLH TRAKPYLNRY
MLPAAYQFVD QLPTTASGKT DRRALGASQA PGTPPQHGAG PAAASTLDPA QAQAQDRADE
EVGDRTMATV TRVWQEVLRL DHDIPVEPTS NFFDMGGSST LLLRLQGKLQ TTLSIPISLQ
EMVRRPTLVQ LVELVHSKVP REGQPPPTPG SRPEEDVVDW AQETTLPAET RYHPPSAPMS
PGGRDILMTG AESFTGIHLL AQLLTSHPSG TIHLLGTHHP WDHAQVFQRL QEYNLLNATL
TPEQILTRLR TIPGSLAEGS HFGLSPRAFE ALGRSIATIY HLASEVSLLK TYHDLKPINT
AAILPLIELA RWGGPSPIHY LSTWSVPHLQ LWTAPPTTPA VVHEASAGHF TPPPTADQGY
FKSRWAAEML LTHAAARGFP VTIYRASAVT GNPTTGLPAP AGDFVRSLIL DMLRHRLVPR
FARESPAPVV VDLVPVNYLT ALLAHLAQRP RAAAAEGPRP AGVEIFHLTN PTPLPLDQLP
GLTGSIRGDA TAGRVVSVDD WLAAVSGSDP AAAAADEDEQ LRVQVAGGYF RRGHQMFALD
RRRTDAALGG VTEGWVDCPP VDANYLRALW LQKV
