ABVS_ASPBC
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 03-AUG-2022, entry version 18.
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}.
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DR EMBL; KV878684; OJJ72250.1; -; Genomic_DNA.
DR SMR; A0A1L9UKS1; -.
DR STRING; 767769.A0A1L9UKS1; -.
DR EnsemblFungi; OJJ72250; OJJ72250; ASPBRDRAFT_675371.
DR VEuPathDB; FungiDB:ASPBRDRAFT_675371; -.
DR OrthoDB; 981769at2759; -.
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:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00685; Trans_IPPS_HT; 1.
DR Gene3D; 1.10.600.10; -; 2.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000092; Polyprenyl_synt.
DR InterPro; IPR033749; Polyprenyl_synt_CS.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SUPFAM; SSF48576; SSF48576; 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
