STBA_STABI
ID STBA_STABI Reviewed; 2220 AA.
AC A0A193PS74;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2016, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Non-reducing polyketide synthase stbA {ECO:0000303|PubMed:26972702};
DE EC=2.3.1.- {ECO:0000269|PubMed:26972702};
DE AltName: Full=Ilicicolin B biosynthesis cluster protein stbA {ECO:0000303|PubMed:26972702};
DE AltName: Full=LL-Z1272-beta biosynthesis cluster protein stbA {ECO:0000303|PubMed:26972702};
GN Name=stbA {ECO:0000303|PubMed:26972702};
OS Stachybotrys bisbyi (Hyalostachybotrys bisbyi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=80385;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DOMAIN, FUNCTION, CATALYTIC ACTIVITY,
RP AND PATHWAY.
RC STRAIN=PYH05-7;
RX PubMed=26972702; DOI=10.1002/cbic.201600087;
RA Li C., Matsuda Y., Gao H., Hu D., Yao X.S., Abe I.;
RT "Biosynthesis of LL-Z1272beta: discovery of a new member of NRPS-like
RT enzymes for aryl-aldehyde formation.";
RL ChemBioChem 17:904-907(2016).
CC -!- FUNCTION: Non-reducing polyketide synthase; part of the cluster that
CC mediates the biosynthesis of LL-Z1272-beta, also known as ilicicolin B,
CC a prenylated aryl-aldehyde produced by several fungi and that serves as
CC a key pathway intermediate for many fungal meroterpenoids
CC (PubMed:26972702). The first step in the pathway is performed by the
CC non-reducing polyketide synthase stbA that produces orsellinic acid by
CC condensing acetyl-CoA with 3 malonyl-CoA units (PubMed:26972702). The
CC prenyltransferase stbC then prenylates orsenilic acid into grifolic
CC acid (PubMed:26972702). Finally, grifolic acid is reduced to ilicicolin
CC B by the NRPS-like protein stbB (PubMed:26972702).
CC {ECO:0000269|PubMed:26972702}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + 2 H(+) + 3 malonyl-CoA = 3 CO2 + 4 CoA +
CC orsellinate; Xref=Rhea:RHEA:62972, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16162, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57384;
CC Evidence={ECO:0000269|PubMed:26972702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62973;
CC Evidence={ECO:0000269|PubMed:26972702};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:26972702}.
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. {ECO:0000305|PubMed:26972702}.
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}.
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DR EMBL; LC125467; BAV19379.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A193PS74; -.
DR SMR; A0A193PS74; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase 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 GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.1200.10; -; 2.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 2.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
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; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF07859; Abhydrolase_3; 1.
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; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF16073; SAT; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; SSF47336; 2.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
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; Transferase.
FT CHAIN 1..2220
FT /note="Non-reducing polyketide synthase stbA"
FT /id="PRO_0000450379"
FT DOMAIN 1634..1711
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1742..1821
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 10..255
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000255"
FT REGION 382..806
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 906..1207
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 1292..1588
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255"
FT REGION 1879..2210
FT /note="Thioesterase (TE) domain"
FT /evidence="ECO:0000250|UniProtKB:Q5ATJ7"
FT ACT_SITE 551
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 993
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 1999
FT /note="For thioesterase activity"
FT /evidence="ECO:0000250|UniProtKB:Q5ATJ7"
FT ACT_SITE 2148
FT /note="For thioesterase activity"
FT /evidence="ECO:0000250|UniProtKB:Q5ATJ7"
FT MOD_RES 1671
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1779
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2220 AA; 237834 MW; 6E333267412A6BEA CRC64;
MARPTTSAAI FSPQNSPPKR SYLAYIRSKL VDDRTLAPLL QAILSLPETW RSLVAARADM
ADMIEAPRLV QSFVDWINTG STDILESELA AIVTLPLLTI IHMVQYYEYL QGAGCSHIEL
LESFDGGVQG HCIGLLSAIV VASAGSEEDL IARAVAGLRL SLAIGAFGDL GEYSTNLRSS
TLVFRLKDMS AADEIVHRFP GTYISTVTDS RTVSMVVPGS QVTDLMAYAD KNGLQPRSVH
IRSRLHDATN TDMAQACREF CDSLEGLPFG AGETLLTSVR SNRTGDCLSD IPESLSTEVI
DTILLSMCNW TKVMRNLVTD LKESSKSQHT LALFGIGDSV PLELFRQNDV DITKFQAVSL
APTAPSPENG LRPTDFFPSD AIAVVGAGFR LPGASTFEEL WEMISEGKTR LEPFRTDRSD
LKGSYRAGQD KEWTKKRNFF GNYVEDIDSF DHSFFGISPR EAKYMDPQQR LLLLTAWEAM
DSAGMLRYHR RERGDNVGCF VGASFNEYVE NTSGYSASAF TATGTIRAFL SGKVSYHFGW
TGPSEVIDTA CSASIVAVHR ACQAIKSGEC PVAVAGGVNL ITGITNYFDL AKASFLSPTG
QCKPFDDSGD GYCRADGVGL VVLKSLSQAV ADGDHIMGVI PSIATNQGGI GAPGITVPDG
IMQRALYKKV LAKSGMRAED ITYVEAHGTG TPVGDPIEIR SIREVFGGAK RPSPLYLGSL
KANVGHSETA AGVASLLKVL TMFREQGIPP IANFKRLNHN IPALETDRMA IPTSQMPWNA
RQRIACINSY GASGSNSALI CSEWPDNNIR DAKDRISAHT PAYPILLSAN SKESLQRYAK
DLATYLTKTN ADKNLGDLAF TLSERRKHHR YRWSTTAADM ASVVDQLQSP LEGVIDSTKT
GKKVVLAFSG QSRTNIGVDP SVIQAYPRFM EHMKQCSSIL QSLGCPDILP YLSQTDPISD
PVILQCGTVS VQISTAKCWM DGGVQVDGIV GHSLGELASL AISGVLSLKD TLTAVYTRAQ
LINLKWGSER GTMMAIHAKV DVIQSVIAKV KAEVSSEDDE VEIACYNSVG SHVIVGKDSS
IAIAEKVLQG DAKYQGLRYQ RVGTSHGFHS RFTKPLLLDL VRFEKTLEFK KPIIPLETCT
QVPFNFESND STYLAHHARD PVYFYDAVQR LEKRLGACAF LEAGWGTPVV SMAKKAVADA
TQHTFQAVTS PATATANLWR EGCSITFWSF LTPKQSMLKP IWTPPYSFDN SKSWLDHVDN
ASVALKAAEA AIAAAATQGS PSTPTEEPRA AQLVRYKGAL GENAHEFGLS TSTERFTKIV
SGHAVKARPL CPASVYMESA IMGCELIGTS GRDKTISFTN ISFQRPLGIN DKLDVKLHLS
KTAKFGDEHW HYSMQSSASA VYSEGDFTMT AGPHQDMELY ALLASDGMVA LRNDPDAEKL
RKRTAYSLFS RVVEYSDLMQ GISDITFGKK AALATIQVPN HPWGSQESSV SGFYDAISLD
TFIQVVGLLI NCSSGTATGD EVYIASSIGN LVVSPTDFQQ AQTWTVYATY STIDSKTLSG
AIFVFNEAGE LVSFGSKIHF HKTSMTKLLR VLDAANPSGA KAAAAPAPRA AFAAPVAAPV
AAAPVAAAAA PVAAAGPSKI PELRALISAY TGVKEADIPD DVAFASLGLD SLSAMELAGE
LESSLGIKVS SDDVTTSTVA SLAKQLPSGG AAPAPVAAAP APVATPAPVA APVAAAPVAA
APAGPSRVGE LRALISAFTG IKEDDIADDV SFGSLGLDSL SAMELASEME STLGLVISSD
DVTSASVSSL SAMLGGGAAD VSAPKSVISS TVASTTPASD FDNQTPDVIT PASECGPELH
EVGSALGIPW KRASPHYSTR FRMETVVYKE IDGTEIPADI YLPAEVPSNP MPIALMIHGG
GHLTLSRRAV RPPQTSYLLA NGILPVSIDY RLAPHVNVVD GSMADTRDAC VWLQKELPEL
MAAKGIIVDP SKYVVIGFST GGTLALTTAW TTAEANVAPP RAILSFYCPV EYDPDHPVLM
GQGTRPRTMT LAQIRETLPN TVAVSHSFNA LDTTKLGWLQ PSDPRSELTL ALIKEENGMS
LLFNGLPEKG EQLPRADPAR CAYFSPLTQV RAGNYNNIPT FMIFGEEDEV APFRKGVEFG
QALKEAGIRG GFHAVKGGKH IFDLALTPGS QGWAEHIAPG YDFIFTELEN ATRGQYILPS
