DRTB_ASPCI
ID DRTB_ASPCI Reviewed; 528 AA.
AC A0A0U5GNT1;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=Drimenol cyclase drtB {ECO:0000303|PubMed:34468074};
DE EC=4.2.3.194 {ECO:0000269|PubMed:34468074};
DE AltName: Full=Drimane-type sesquiterpene ester biosynthesis cluster protein B {ECO:0000303|PubMed:34468074};
DE AltName: Full=Drimenol synthase {ECO:0000305};
GN Name=drtB {ECO:0000303|PubMed:34468074}; ORFNames=ASPCAL02978;
OS Aspergillus calidoustus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=454130;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF006504;
RX PubMed=26966204; DOI=10.1128/genomea.00102-16;
RA Horn F., Linde J., Mattern D.J., Walther G., Guthke R., Scherlach K.,
RA Martin K., Brakhage A.A., Petzke L., Valiante V.;
RT "Draft genome sequences of fungus Aspergillus calidoustus.";
RL Genome Announc. 4:0-0(2016).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=34468074; DOI=10.1002/anie.202108970;
RA Huang Y., Hoefgen S., Valiante V.;
RT "Biosynthesis of fungal drimane-type sesquiterpene esters.";
RL Angew. Chem. Int. Ed. 60:23763-23770(2021).
CC -!- FUNCTION: Drimenol cyclase; part of the gene cluster that mediates the
CC biosynthesis of various drimane-type sesquiterpene esters, compounds
CC that exhibit diverse biological activities and are widely present in
CC eukaryotes (PubMed:34468074). The pathway begins with the synthesis of
CC the backbone drimenol by the terpene cyclase drtB using farnesyl
CC pyrophosphate (FPP) as substrate (PubMed:34468074). The cytochrome P450
CC monooxygenase drtD is then responsible for the hydroxylations at C-6,
CC C-9 and C-12, as well as the oxidation of hydroxyl groups at C-6 and C-
CC 11 to a ketone and an aldehyde, respectively (PubMed:34468074). Then,
CC the biosynthesis can go in two directions, either the hydroxylated
CC drimenol is further hydroxylated at C-2 and C-3 by an enzyme(s) not
CC associated with the drt cluster, or the FAD-binding oxidoreductase drtC
CC further oxidizes C-11 or C-12 to form the butyrolactone ring
CC (PubMed:34468074). DrtB, drtD and drtC are solely responsible for the
CC formation of the different drimane structures observed during drimane
CC sesquiterpenes biosynthesis (PubMed:34468074). The polyketide synthase
CC drtA synthesizes different lengths (C6 and C8) of PKS chains, which are
CC then oxidized to varying degrees by the short-chain dehydrogenase drtF
CC (PubMed:34468074). Finally, these PKS chains are transferred onto
CC drimane sesquiterpenes by the acyltransferase drtE, forming the
CC sesquiterpene esters (PubMed:34468074). In addition to the different
CC fatty acyl-CoA chains produced by drtA, drtE is also able to use
CC cinnamoyl-CoA as a substrate (PubMed:34468074).
CC {ECO:0000269|PubMed:34468074}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = (5S,9S,10S)-drim-7-en-11-
CC ol + diphosphate; Xref=Rhea:RHEA:28290, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:61148, ChEBI:CHEBI:175763;
CC EC=4.2.3.194; Evidence={ECO:0000269|PubMed:34468074};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28291;
CC Evidence={ECO:0000269|PubMed:34468074};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:34468074}.
CC -!- DISRUPTION PHENOTYPE: Abolished the drimane sesquiterpenes
CC biosynthesis. {ECO:0000269|PubMed:34468074}.
CC -!- MISCELLANEOUS: The various drimane-type sesquiterpene esters produced
CC by the A.calidoustus drt cluster include asperiene C, asperiene A, (6-
CC Strobilactone-B) ester of (E,E)-6-carbonyl-7-hydroxy-2,4-octadienoic
CC acid, ustusolate A, ustusolate C, ustusolide E, ustusoic acid A,
CC (2'E,4'E)-6-(1'-carboxyhexa-2',4',-diene)-9-hydroxy-drim-7-ene-11,12-
CC olide, RES-1149-2, as well as the 3 newly identified compounds
CC calidoustene A, calidoustene B and calidoustene C.
CC {ECO:0000269|PubMed:34468074}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC {ECO:0000305}.
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DR EMBL; CDMC01000002; CEN60542.1; -; Genomic_DNA.
DR EnsemblFungi; CEN60542; CEN60542; ASPCAL02978.
DR OrthoDB; 841906at2759; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000054771; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProt.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR Pfam; PF13419; HAD_2; 1.
DR PRINTS; PR00413; HADHALOGNASE.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
PE 1: Evidence at protein level;
KW Lyase; Reference proteome.
FT CHAIN 1..528
FT /note="Drimenol cyclase drtB"
FT /id="PRO_0000454532"
SQ SEQUENCE 528 AA; 58757 MW; 707FE71F4004EAA8 CRC64;
MVRALILDLG DVLFNWDAPA STPISRKTLG QMLHSEIWGE YERGHLTEDE AYNALAKRYS
CEAKDVAHTF VLARESLRLD TKFKTFLQTL KQNANGSLRV YGMSNISKPD FEVLLGKADD
WTLFDKIFPS GHVGMRKPDL AFFRYVLKDI STPVEDVVFV DDNLDNVTSA RSLGMRSVLF
HKKDEVQRQL TNIFGSPAER GLEYLSANKT NLQSATTTDI PIQDNFGQLL ILEATEDPSL
VRMEPGKRTW NFFIGSPSLT TDTFPDDLDT TSLALSIVPT SPDVVNSVID EIISRRDKDG
IVPTYFDNTR PRVDPIVCVN VLSMFAKYGR EHDLPATVAW VRDVLYHRAY LGGTRYYGSA
EAFLFFFTRF VRNLRPGTLK QDLHALLSER VRERLNTPVD ALALSMRIQA CHALGFDAPA
DIATLITMQD EDGGWPAAVI YKYGAGGLGI TNRGVSTAFA VKAITGSPVK TETNIGGDGA
RAVSAMSSLE ARRLQPISSV GDWVRFIIAS LHVHLAWLWN VLLLSKVV
