ANEC_ASPA1
ID ANEC_ASPA1 Reviewed; 442 AA.
AC A0A1L9WUI2;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=Terpene cyclase aneC {ECO:0000303|PubMed:31618514};
DE EC=4.2.3.- {ECO:0000269|PubMed:31618514};
DE AltName: Full=Aculenes biosynthesis cluster protein C {ECO:0000303|PubMed:31618514};
GN Name=aneC {ECO:0000303|PubMed:31618514}; ORFNames=ASPACDRAFT_60731;
OS Aspergillus aculeatus (strain ATCC 16872 / CBS 172.66 / WB 5094).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=690307;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 16872 / CBS 172.66 / WB 5094;
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=31618514; DOI=10.1002/anie.201910200;
RA Lee C.F., Chen L.X., Chiang C.Y., Lai C.Y., Lin H.C.;
RT "The biosynthesis of norsesquiterpene aculenes requires three cytochrome
RT P450 enzymes to catalyze a stepwise demethylation process.";
RL Angew. Chem. Int. Ed. 58:18414-18418(2019).
CC -!- FUNCTION: Terpene cyclase; part of the gene cluster that mediates the
CC biosynthesis of aculenes, a unique type of norsesquiterpenes that
CC contain a nordaucane skeleton linked to an L-proline moiety and are of
CC mixed biosynthetic origin (PubMed:31618514). The pathway begins with
CC the synthesis of dauca-4,7-diene by the terpene cyclase aneC using
CC farnesyl pyrophosphate (FPP) as substrate (PubMed:31618514). The
CC cytochrome P450 monooxygenase aneF then performs the initial oxidation
CC at C-12 of dauca-4,7-diene to yield asperaculane D (PubMed:31618514).
CC Asperaculane D is substrate of the cytochrome P450 monooxygenase aneD
CC for C-10 hydroxylation to yield asperaculane E (PubMed:31618514). The
CC cytochrome P450 monooxygenase aneG then converts asperaculane E into
CC aculene D via C-2 oxidation (PubMed:31618514). The monomodular
CC nonribosomal peptide synthtase aneB adenylates L-proline and the
CC thiohydrolase aneE transfers this activated L-proline derivative to
CC aculenes D and C to produce respectively aculenes B and A
CC (PubMed:31618514). The dioxygenase aneA converts aculene D into aculene
CC C, and aculene B into aculene A by introducing the 5,6-alkene moiety
CC (PubMed:31618514). Asperculanes A, B, C and F, as well as 14-prolyl
CC asperculane C, might be shunt products of the pathway
CC (PubMed:31618514). {ECO:0000269|PubMed:31618514}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = dauca-4,7-diene + diphosphate;
CC Xref=Rhea:RHEA:65072, ChEBI:CHEBI:33019, ChEBI:CHEBI:155906,
CC ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:31618514};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65073;
CC Evidence={ECO:0000269|PubMed:31618514};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9UR08};
CC Note=Binds 3 Mg(2+) ions per monomer. {ECO:0000250|UniProtKB:Q9UR08};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:31618514}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9UR08}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of aculene or any
CC intermediates. {ECO:0000269|PubMed:31618514}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; KV878977; OJJ99914.1; -; Genomic_DNA.
DR RefSeq; XP_020056254.1; XM_020203588.1.
DR AlphaFoldDB; A0A1L9WUI2; -.
DR SMR; A0A1L9WUI2; -.
DR EnsemblFungi; OJJ99914; OJJ99914; ASPACDRAFT_60731.
DR GeneID; 30977402; -.
DR VEuPathDB; FungiDB:ASPACDRAFT_60731; -.
DR OrthoDB; 1143139at2759; -.
DR Proteomes; UP000184546; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..442
FT /note="Terpene cyclase aneC"
FT /id="PRO_0000449092"
FT BINDING 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 327
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 331
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 334
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 335
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 419..420
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
SQ SEQUENCE 442 AA; 50834 MW; 4AA01E011DD6B5D2 CRC64;
MTPDLVARFW LVELHVRLPA WLRGITSASA SVAVKRPGSS KKPLEPAPQP APYKPTHYRH
IIYAYDVMEE KCEIPVLEHD PFDFLDPQKT LVPPENTILI DPVAVGLPWF STMKGTPQCI
HWREAEAAGL ELIEQVMAAR GAGAVIPEKL KTSDQRRKMM ELVETAVTIC IYLYAVSDAA
RIRVLTKSIV FLFLHDDVME SKANAEGNSI LEGWDTDTFK ANELEGESRN DIFLDFCREA
IALDPVLGLE LMQDTVRWAR YSRVNSTKAD KTHATWQDFR DFRELDIAYD FMITAVRFGA
AILYDPAERP VFEWIEKLYI RHCLYINDLY SYEKEFREHQ QEGAPLHNSV HMIEQVLSVP
PGSAKAILRS VLWDCERQVR EEYVRLMQLP ELTHTQKVYL QRLIESFAGN YMYSMSTYRY
ARLSGKLIGP PPEDCLLKNY VQ
