STBC_STABI
ID STBC_STABI Reviewed; 333 AA.
AC A0A193PS58;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2016, sequence version 1.
DT 03-AUG-2022, entry version 11.
DE RecName: Full=Prenyltransferase stbC {ECO:0000303|PubMed:26972702};
DE EC=2.5.1.- {ECO:0000269|PubMed:26972702};
DE AltName: Full=Ilicicolin B biosynthesis cluster protein stbC {ECO:0000303|PubMed:26972702};
DE AltName: Full=LL-Z1272-beta biosynthesis cluster protein stbC {ECO:0000303|PubMed:26972702};
GN Name=stbC {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], FUNCTION, CATALYTIC ACTIVITY, AND
RP 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: Prenyltransferase; part of the cluster that mediates the
CC biosynthesis of LL-Z1272-beta, also known as ilicicolin B, a prenylated
CC aryl-aldehyde produced by several fungi and that serves as a key
CC pathway intermediate for many fungal meroterpenoids (PubMed:26972702).
CC The first step in the pathway is performed by the non-reducing
CC polyketide synthase stbA that produces orsellinic acid by condensing
CC 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=(2E,6E)-farnesyl diphosphate + orsellinate = diphosphate +
CC ilicicolinate B; Xref=Rhea:RHEA:63012, ChEBI:CHEBI:16162,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:146152, ChEBI:CHEBI:175763;
CC Evidence={ECO:0000269|PubMed:26972702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63013;
CC Evidence={ECO:0000269|PubMed:26972702};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:26972702}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000305}.
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DR EMBL; LC125467; BAV19381.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A193PS58; -.
DR SMR; A0A193PS58; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd13959; PT_UbiA_COQ2; 1.
DR Gene3D; 1.10.357.140; -; 1.
DR InterPro; IPR039653; Prenyltransferase.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR InterPro; IPR044878; UbiA_sf.
DR PANTHER; PTHR11048; PTHR11048; 1.
DR Pfam; PF01040; UbiA; 1.
PE 1: Evidence at protein level;
KW Magnesium; Membrane; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..333
FT /note="Prenyltransferase stbC"
FT /id="PRO_0000450381"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 333 AA; 36424 MW; B8F9CE43D174DF3D CRC64;
MPATRTPIHP EAAAYKNPRY QSGPLSVIPK SFVPYCELMR LELPHGNFLG YFPHLVGLLY
GSSASPARLP ANEVAFQAVL YIGWTFFMRG AGCAWNDVVD QDFDRKTTRC RVRPVARGAV
STTSANIFGF AMVALAFACI SPLPAECQRL GLMTTVLSII YPFCKRVTNF AQVILGMTLA
INFILAAYGA GLPAIEAPYT VPTICVTTAI TLLVVFYDVV YARQDTADDL KSGVKGMAVL
FRNYVEILLT SITLVIAGLI ATTGVLVDNG PYFFVFSVAG LLAALLAMIG GIRYRIFHTW
NSYSGWFYAL AIFNLLGGYL IEYLDQVPML NKA
