ID   PKS24_BYSSP             Reviewed;        2149 AA.
AC   P9WET9;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   03-AUG-2022, sequence version 1.
DT   03-AUG-2022, entry version 1.
DE   RecName: Full=Non-reducing polyketide synthase PvBS090_009107 {ECO:0000303|PubMed:33989788};
DE            EC=2.3.1.- {ECO:0000269|PubMed:33989788};
DE   AltName: Full=Pigment biosynthesis cluster 24 polyketide synthase {ECO:0000303|PubMed:33989788};
GN   ORFNames=PvBS090_009107;
OS   Byssochlamys spectabilis (Paecilomyces variotii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX   NCBI_TaxID=264951;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28408692; DOI=10.1128/genomea.01602-16;
RA   Singh N.K., Blachowicz A., Romsdahl J., Wang C., Torok T.,
RA   Venkateswaran K.;
RT   "Draft genome sequences of several fungal strains selected for exposure to
RT   microgravity at the international space station.";
RL   Genome Announc. 5:0-0(2017).
RN   [2]
RP   FUNCTION, DOMAIN, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=IMV 00236;
RX   PubMed=33989788; DOI=10.1016/j.fgb.2021.103567;
RA   Lim S., Bijlani S., Blachowicz A., Chiang Y.M., Lee M.S., Torok T.,
RA   Venkateswaran K., Wang C.C.C.;
RT   "Identification of the pigment and its role in UV resistance in
RT   Paecilomyces variotii, a Chernobyl isolate, using genetic manipulation
RT   strategies.";
RL   Fungal Genet. Biol. 152:103567-103567(2021).
CC   -!- FUNCTION: Non-reducing polyketide synthase; part of the gene cluster 24
CC       that mediates the biosynthesis of a pigment with an aromatic structure
CC       protecting the pigmented fungus from both ionizing and non-ionizing
CC       radiations based on a mechanism similar to melanin, that is, free
CC       radical quenching and spherical spatial arrangement (PubMed:33989788).
CC       Catalyzes the biosynthesis of the gamma-naphthopyrone precursor YWA1,
CC       via condensation of one acetyl-CoA starter unit with 6 malonyl-CoA
CC       units (PubMed:33989788). YWA1 is probably further processed by the
CC       additionnal enzymes present within the cluster 24, however these
CC       additionnal steps have not been characterized yet (Probable). YWA1 is
CC       not converted to DHN-melanin in Byssochlamys spectabilis since the use
CC       of the DHN-melanin pathway inhibitor pyroquilon does not result in a
CC       loss of pigmentation (PubMed:33989788). {ECO:0000269|PubMed:33989788,
CC       ECO:0000305|PubMed:33989788}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + 6 H(+) + 6 malonyl-CoA = 6 CO2 + 7 CoA + H2O +
CC         YWA1; Xref=Rhea:RHEA:62652, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:57384, ChEBI:CHEBI:133763;
CC         Evidence={ECO:0000269|PubMed:33989788};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62653;
CC         Evidence={ECO:0000269|PubMed:33989788};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:33989788}.
CC   -!- PATHWAY: Pigment biosynthesis. {ECO:0000269|PubMed:33989788}.
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 2 acyl-carrier protein (ACP) domains
CC       that serve as the tethers of the growing and completed polyketide via
CC       their phosphopantetheinyl arm. {ECO:0000250|UniProtKB:Q5B0D0}.
CC   -!- DOMAIN: The release of the polyketide chain from the non-reducing
CC       polyketide synthase is mediated by the thioesterase (TE) domain
CC       localized at the C-ter of the protein. {ECO:0000250|UniProtKB:Q5ATJ7}.
CC   -!- DISRUPTION PHENOTYPE: Leads to the loss of pigmentation and increased
CC       sensitivity to UV-C radiations. {ECO:0000269|PubMed:33989788}.
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DR   EMBL; MSJH02000000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE   1: Evidence at protein level;
KW   Multifunctional enzyme; Phosphopantetheine; Phosphoprotein; Repeat;
KW   Transferase.
FT   CHAIN           1..2149
FT                   /note="Non-reducing polyketide synthase PvBS090_009107"
FT                   /id="PRO_0000455748"
FT   DOMAIN          1649..1726
FT                   /note="Carrier 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   DOMAIN          1769..1846
FT                   /note="Carrier 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          8..244
FT                   /note="N-terminal acylcarrier protein transacylase domain
FT                   (SAT)"
FT                   /evidence="ECO:0000255"
FT   REGION          378..809
FT                   /note="Ketosynthase (KS) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          911..1231
FT                   /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          1290..1604
FT                   /note="Product template (PT) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          1875..2147
FT                   /note="Thioesterase (TE) domain"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        547
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        1000
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        1965
FT                   /note="For thioesterase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q03149"
FT   MOD_RES         1686
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         1806
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2149 AA;  234807 MW;  4C5CE89A207DA8C0 CRC64;
     MRVTSRVYLF GDQTGEFETG LRQLLQAKNN SLLTSFFERC FYALRQEVSK LPPSQRQIFP
     RFTSIVDLLA RHREFGPNPA LESALTCIYH FACFINHYGD GGHAYPSASE SHIIGLCTGL
     LASAAVSSSR TVGELIPAAI ETVTVSLRLG LCVLRTRDLI DRSYEKSQSW SMVVSGLNEE
     EVGALIHGFC QRKSISPSSR PYISAVNTHS LTISAPPTIL QEFTNVCLSK ENRPVRVPVH
     APYHAPHLYD RRDVTSILES WPKGELANYT PRIPVLSSET GEIILARNLH ELLGIALEEI
     LLRKLCWDKV QDGYASMLKR TSSAACRIFP IASAASHGLS AALKRTGVPD VEVDNTISES
     AKTCDNENST GRTEQSKIAI IGLSGRFPDA PSPEHFWDLL YKGLDVHRVV PPDRWDVKAH
     VDPTGKIRNT SKVPYGCWIE EPGLFDPRFF NMSPREALQA DPAQRLALVT AYEALEQAGF
     VPDSTPSTQK DRVGIFYGMT SDDYREVNSG QDIDTYFIPG GNRAFTPGRI NYHFKFSGPS
     VSVDTACSSS LAAIHLACNS LWRNDCDTAI AGGTNVLTNP DNFAGLDRGH FLSAKGNCNT
     FDDEADGYCR ADAVGTVVLK RLEDAQADKD PILGVILGAY TNHSAEAVSM TRPHVGAQAF
     IFNKLLNEAN VSPRDVGYIE MHGTGTQAGD AVEMKSVLDI FAPDYTRGPS QSLYLGSAKA
     NIGHAESASG VSSLIKVLLM LKANTIPPHC GIKTKINHNF PTDFKERNVH IAFKPTSWER
     PQDGKRRLFV NNFSAAGGNT ALLIEDAPLS TVSGAPDSRS THIVAVSARS QSSLRNNIRS
     LMKYVSELDG QIGGENFLGK LSYTTTARRI HHQFRTMVSG SSLKGIQEAL SSAASRDSFT
     PIPASTPSIG FVFTGQGAQY TGMGQQLYSS CSQFRDNIDR FDSIARSQGF PSIVPLIDGS
     VPVEEMSPVV TQLGTTCLQM AMTRYWMSLG VKPAFVLGHS LGNYAALNAA GVLTTSDTIY
     LSGRRAQLLQ EKCQVGTHSM LAIKANLAQI KPFLDDDAYE VACINAPGET VISGLSANID
     VLSEKLTAEG LKSTKLRVPY AFHSAQVEPI LESLGEVAQG VTFHKPSIPV VSALLGEVIN
     EDNWDALGPR YLQRHCRETV NLLAALEATR HAKLMNEKTI WIEVGSHPIC SGMIKGTLGP
     QANTVASLRR NEDTWKVLCN SLSAIYLAGV DIQWKEYHGD FTSSHQVLQL PAYSWDNKNY
     YIPYNNNFCL TKGDPTVAKI EAAPTSQFHT TSVQRIVETR DEGSKAVVVM ESDLSDPLLN
     PVIQGHKVNG AALCPSSLYA DIAQTLGEYL IENYNPALRG SGLDVCDMTV PKPLIAKNSG
     PQLFRAMATA DWEERKANIQ IYSVKSDGKK IMDHASCLVK FSDTHLWEAD WKRHSYLIKR
     SIERLQKSVE EGQSHRMHRG MFYKLFSALV DYGDNYKSVE EVVLDSEEYE ATARVKFQAK
     SGNFHRNPFW IDSIGHLTGF VMNANDATDS QSQVYVNHGW DFMRCLKKFS PDTTYRTYVK
     MQPWQGTIYA GDVYAFDGDE IVAVYGGVKF QGVPRQVLNT VLPPAGGSKA APRTTARAVP
     PPPINVEKPK SSVEAKAVSK AVPGDPVKSA GPSVLVQALK ILAEEIGVSE AELSDDLVFA
     DYGVDSLLSL TITGKFREEL NMDLESSTFI DHPTVKDLKQ LLSQASPSDS SDSSEESHYS
     FRDSSSTEPS TPGTPAFFSP KRGSVVTNVG ESETIKTIRL TLSEEIGVSP DEITGDANLA
     EMGMDSLLSL TVLGRLRETL DIELPSDFFI ENPTMDAVET ALDLKPKAEP IPSELPVPIQ
     TAAGDEINGV IKANSTHPPA TSILLQGNPK KATKTLFLFP DGSGSATSYA TLPAVSSDVC
     VYGLNCPYMK NPENLKCGLD ELTMPYVAEI RRRQPKGPYS FGGWSAGGIC AYDAARYLIL
     EEGEKVERLL LLDSPFPIGL EKLPPRLYSF FNTIGLFGEG KTPPPKWLLP HFLAFIDSLD
     AYNAVPFPFS DPELGENMPK TYLIWAKDGV CGKPGDPRPD PPTDGSKDPR EMLWLLNDRT
     DMGPNGWDTL VGPNNVAAIE AIEGADHFTM MKGDKAAKLS AFIGRAMAS