ID ABVS_ASPBC Reviewed; 695 AA. AC A0A1L9UKS1; DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2017, sequence version 1. DT 27-MAR-2024, entry version 27. DE RecName: Full=Variediene synthase {ECO:0000303|PubMed:31476106}; DE Short=VS {ECO:0000303|PubMed:31476106}; DE Includes: DE RecName: Full=Terpene cyclase {ECO:0000303|PubMed:31476106}; DE EC=4.2.3.- {ECO:0000269|PubMed:31476106}; DE Includes: DE RecName: Full=Geranylgeranyl diphosphate synthase {ECO:0000303|PubMed:31476106}; DE Short=GGDP synthase {ECO:0000303|PubMed:31476106}; DE Short=GGS {ECO:0000303|PubMed:31476106}; DE EC=2.5.1.29 {ECO:0000269|PubMed:31476106}; GN Name=AbVS {ECO:0000303|PubMed:31476106}; ORFNames=ASPBRDRAFT_675371; OS Aspergillus brasiliensis (strain CBS 101740 / IMI 381727 / IBT 21946). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus. OX NCBI_TaxID=767769; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 101740 / IMI 381727 / IBT 21946; 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, CATALYTIC ACTIVITY, DOMAIN, AND PATHWAY. RX PubMed=31476106; DOI=10.1002/cbic.201900462; RA Rinkel J., Steiner S.T., Bian G., Chen R., Liu T., Dickschat J.S.; RT "A family of related fungal and bacterial di- and sesterterpenes: studies RT on fusaterpenol and variediene."; RL ChemBioChem 21:486-491(2020). CC -!- FUNCTION: Bifunctional terpene synthase converts DMAPP and IPP, and CC also GGPP, into variediene as a single product (PubMed:31476106). The CC C-terminal prenyltransferase domain of AbVS catalyzes formation of CC GGPP, whereas the N-terminal terpene cyclase domain catalyzes the CC cyclization of GGPP to variediene (PubMed:31476106). CC {ECO:0000269|PubMed:31476106}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = CC (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate; CC Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, CC ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29; CC Evidence={ECO:0000269|PubMed:31476106}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17654; CC Evidence={ECO:0000269|PubMed:31476106}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P9WEV7}; CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. CC {ECO:0000269|PubMed:31476106}. CC -!- SUBUNIT: Hexamer. {ECO:0000250|UniProtKB:A2PZA5}. CC -!- DOMAIN: The conserved DDXXD motifs as well as the NSE/DTE motif are CC important for the catalytic activity, presumably through binding to CC Mg(2+). {ECO:0000305|PubMed:31476106}. CC -!- SIMILARITY: In the N-terminal section; belongs to the terpene synthase CC family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the FPP/GGPP synthase CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KV878684; OJJ72250.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1L9UKS1; -. DR SMR; A0A1L9UKS1; -. DR STRING; 767769.A0A1L9UKS1; -. DR VEuPathDB; FungiDB:ASPBRDRAFT_675371; -. DR OMA; VKPCYAA; -. DR OrthoDB; 5770at2759; -. DR UniPathway; UPA00213; -. DR Proteomes; UP000184499; 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 GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0046165; P:alcohol biosynthetic process; IEA:UniProt. DR GO; GO:0043386; P:mycotoxin biosynthetic process; IEA:UniProt. DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd00685; Trans_IPPS_HT; 1. DR Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 2. DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf. DR InterPro; IPR000092; Polyprenyl_synt. DR InterPro; IPR033749; Polyprenyl_synt_CS. DR PANTHER; PTHR12001; GERANYLGERANYL PYROPHOSPHATE SYNTHASE; 1. DR PANTHER; PTHR12001:SF72; THIJ_PFPI FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_3G01210)-RELATED; 1. DR Pfam; PF00348; polyprenyl_synt; 1. DR Pfam; PF19086; Terpene_syn_C_2; 1. DR SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1. DR SUPFAM; SSF48576; Terpenoid synthases; 2. DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1. DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1. PE 1: Evidence at protein level; KW Isoprene biosynthesis; Lyase; Magnesium; Metal-binding; KW Multifunctional enzyme; Reference proteome; Repeat; Transferase. FT CHAIN 1..695 FT /note="Variediene synthase" FT /id="PRO_0000453636" FT REGION 1..23 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 7..332 FT /note="Terpene cyclase" FT /evidence="ECO:0000305|PubMed:31476106" FT REGION 353..392 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 98..102 FT /note="DDXXD 1" FT /evidence="ECO:0000305|PubMed:31476106" FT MOTIF 228..236 FT /note="NSE/DTE" FT /evidence="ECO:0000305|PubMed:31476106" FT MOTIF 454..458 FT /note="DDXXD 2" FT /evidence="ECO:0000305|PubMed:31476106" FT COMPBIAS 355..385 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 98 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q40577" FT BINDING 98 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q40577" FT BINDING 98 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:A2PZA5" FT BINDING 184..187 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:A2PZA5" FT BINDING 228 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:A2PZA5" FT BINDING 232..236 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:A2PZA5" FT BINDING 324..325 FT /ligand="substrate" FT /evidence="ECO:0000305|PubMed:31476106" FT BINDING 415 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000250|UniProtKB:Q12051" FT BINDING 418 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000250|UniProtKB:Q12051" FT BINDING 447 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000250|UniProtKB:Q12051" FT BINDING 454 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:Q12051" FT BINDING 454 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:Q12051" FT BINDING 458 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:Q12051" FT BINDING 458 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="4" FT /evidence="ECO:0000250|UniProtKB:Q12051" FT BINDING 463 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000250|UniProtKB:Q12051" FT BINDING 464 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000250|UniProtKB:Q12051" FT BINDING 541 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000250|UniProtKB:Q12051" FT BINDING 542 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000250|UniProtKB:Q12051" FT BINDING 579 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000250|UniProtKB:Q12051" FT BINDING 586 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000250|UniProtKB:Q12051" FT BINDING 595 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000250|UniProtKB:Q12051" FT BINDING 605 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000250|UniProtKB:Q12051" SQ SEQUENCE 695 AA; 79464 MW; A4BB6FE83441FF21 CRC64; MVPTSLSPDD TSDPVPRSSS DIQGFCHNYP LRRHKYEDQA NKGSQQCRDD WEQYIGPIER WGCGNPWEGH FAAVVLPFCR PDRIAIISYC FEYAFMYDNV VESAAKSTVN INRDDIALDE TEYRTVRSVT GTKQIQSKML LDLLSIDPVC AEVVIDSWKT MIDTTVKQDK TRTFSNLEEY VDFRIIDTGA PFVDTLMRFG MNILLTPEEE ELVAPIVKPC YAALGLANDY FSFDIEWEEF QQPESNQSTM TNAVWLFMQW HQVDEQEAKR RVRQVTNDYE REYQQRVRDF ISGEGKSNTK LQLYLTALGY QIPGNIAWSL RCPRYHPWLC EEGSALLRAS MDEARDVCNE GKRRSISGDS ISSESSVWSG ASDRSARSSV SSAPSLDEGK EPDRVMLGTE HLLGPAEYIA SLPSKGVREA FIDALNVWLV LPDRFVGVIK SIAKTLHNAS LMLDDIEDGS PLRRGQPATH TIFGQALTIN SANFVLIQAM DQVRQLEDSR CLDIFVEEMR NLFIGQSFDL YWTRQDECPS EEEYREMIRQ KTGGLFRLVA RLMMQKATLK KNQHISLEPL VDLMGEYFQI RDDYKNLTEE YTGQKGFCED LDEGKFSFPL IHAHKLLPEW SEIRLLLQQG RQSGGLDVTQ KQLVLGRLHD SGSMAYTEKT LRGLMGEIRL RIDQVEKESG CSNWVLKLLV HRLEV //