ID TATC6_HYPAT Reviewed; 386 AA. AC A0A5S9I252; DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot. DT 22-APR-2020, sequence version 1. DT 25-MAY-2022, entry version 9. DE RecName: Full=Terpene cyclase 6 {ECO:0000303|PubMed:31418991}; DE EC=4.2.3.- {ECO:0000269|PubMed:31418991}; DE EC=4.2.3.104 {ECO:0000269|PubMed:31418991}; DE EC=4.2.3.137 {ECO:0000269|PubMed:31418991}; DE EC=4.2.3.157 {ECO:0000269|PubMed:31418991}; DE EC=4.2.3.182 {ECO:0000269|PubMed:31418991}; DE EC=4.2.3.57 {ECO:0000269|PubMed:31418991}; DE AltName: Full=Sesquiterpene synthase 6 {ECO:0000303|PubMed:31418991}; GN Name=tatc6 {ECO:0000303|PubMed:31418991}; OS Hypocrea atroviridis (Trichoderma atroviride). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma. OX NCBI_TaxID=63577; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND RP DISRUPTION PHENOTYPE. RC STRAIN=FKI-3849; RX PubMed=31418991; DOI=10.1002/anie.201907964; RA Murai K., Lauterbach L., Teramoto K., Quan Z., Barra L., Yamamoto T., RA Nonaka K., Shiomi K., Nishiyama M., Kuzuyama T., Dickschat J.S.; RT "An unusual skeletal rearrangement in the biosynthesis of the sesquiterpene RT trichobrasilenol from Trichoderma."; RL Angew. Chem. Int. Ed. 58:15046-15050(2019). CC -!- FUNCTION: Terpene cyclase that is able to convert FPP into a mixture of CC sesquiterpene hydrocarbons and alcohols (PubMed:31418991). The main CC product is trichobrasilenol (PubMed:31418991). Additionally, side CC products include alpha-humulene, caryophyllene, 2-epi-caryophyllene, CC african-3-ene, african-1-ene, isoafricanol and pristinol CC (PubMed:31418991). Does not accept GPP, GGPP, and GFPP as substrates CC (PubMed:31418991). {ECO:0000269|PubMed:31418991}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = diphosphate + CC trichobrasilenol; Xref=Rhea:RHEA:66644, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:167379, ChEBI:CHEBI:175763; CC Evidence={ECO:0000269|PubMed:31418991}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66645; CC Evidence={ECO:0000269|PubMed:31418991}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E,6E)-farnesyl diphosphate = alpha-humulene + diphosphate; CC Xref=Rhea:RHEA:31895, ChEBI:CHEBI:5768, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:175763; EC=4.2.3.104; CC Evidence={ECO:0000269|PubMed:31418991}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31896; CC Evidence={ECO:0000269|PubMed:31418991}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E,6E)-farnesyl diphosphate = (-)-(E)-beta-caryophyllene + CC diphosphate; Xref=Rhea:RHEA:28294, ChEBI:CHEBI:10357, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.57; CC Evidence={ECO:0000269|PubMed:31418991}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28295; CC Evidence={ECO:0000269|PubMed:31418991}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E,6E)-farnesyl diphosphate = (E)-2-epi-beta-caryophyllene + CC diphosphate; Xref=Rhea:RHEA:34703, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:68667, ChEBI:CHEBI:175763; EC=4.2.3.137; CC Evidence={ECO:0000269|PubMed:31418991}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34704; CC Evidence={ECO:0000269|PubMed:31418991}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = (+)-isoafricanol + CC diphosphate; Xref=Rhea:RHEA:53616, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:137522, ChEBI:CHEBI:175763; CC EC=4.2.3.157; Evidence={ECO:0000269|PubMed:31418991}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53617; CC Evidence={ECO:0000269|PubMed:31418991}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = (+)-(2S,3R,9R)-pristinol CC + diphosphate; Xref=Rhea:RHEA:54372, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:138165, ChEBI:CHEBI:175763; CC EC=4.2.3.182; Evidence={ECO:0000269|PubMed:31418991}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54373; CC Evidence={ECO:0000269|PubMed:31418991}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E,6E)-farnesyl diphosphate = african-3-ene + diphosphate; CC Xref=Rhea:RHEA:66648, ChEBI:CHEBI:33019, ChEBI:CHEBI:167380, CC ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:31418991}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66649; CC Evidence={ECO:0000269|PubMed:31418991}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E,6E)-farnesyl diphosphate = african-1-ene + diphosphate; CC Xref=Rhea:RHEA:66652, ChEBI:CHEBI:33019, ChEBI:CHEBI:167381, CC ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:31418991}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66653; CC Evidence={ECO:0000269|PubMed:31418991}; 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: Sesquiterpene biosynthesis. {ECO:0000269|PubMed:31418991}. CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9UR08}. CC -!- DOMAIN: The 2 conserved active-site motifs D(D/E)XX(D/E) and NSE are CC required for coordinating the divalent metal ions that stabilize the CC PPi moiety of the substrate. {ECO:0000250|UniProtKB:Q9UR08}. CC -!- DOMAIN: The C-terminal WxxxxxRY motif is frequently found in terpene CC synthases and is important to guide product formation. CC {ECO:0000250|UniProtKB:P9WEY7}. CC -!- DISRUPTION PHENOTYPE: Abolishes the production of koraiol. CC {ECO:0000269|PubMed:31418991}. CC -!- SIMILARITY: Belongs to the terpene synthase 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; LC484924; BBK61014.1; -; Genomic_DNA. DR AlphaFoldDB; A0A5S9I252; -. DR SMR; A0A5S9I252; -. DR GO; GO:0080016; F:(-)-E-beta-caryophyllene synthase activity; IEA:UniProtKB-EC. DR GO; GO:0080017; F:alpha-humulene synthase activity; IEA:UniProtKB-EC. 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 InterPro; IPR034686; Terpene_cyclase-like_2. DR SFLD; SFLDG01020; Terpene_Cyclase_Like_2; 1. DR SUPFAM; SSF48576; SSF48576; 1. PE 1: Evidence at protein level; KW Lyase; Magnesium; Metal-binding. FT CHAIN 1..386 FT /note="Terpene cyclase 6" FT /id="PRO_0000452513" FT REGION 366..367 FT /note="Substrate-binding" FT /evidence="ECO:0000250|UniProtKB:Q9UR08" FT MOTIF 128..132 FT /note="D(D/E)XX(D/E) motif" FT /evidence="ECO:0000250|UniProtKB:Q9UR08" FT MOTIF 276..284 FT /note="NSE motif" FT /evidence="ECO:0000250|UniProtKB:P9WEY7" FT MOTIF 360..367 FT /note="WxxxxxRY motif" FT /evidence="ECO:0000250|UniProtKB:P9WEY7" FT METAL 128 FT /note="Magnesium 1" FT /evidence="ECO:0000250|UniProtKB:Q9UR08" FT METAL 128 FT /note="Magnesium 2" FT /evidence="ECO:0000250|UniProtKB:Q9UR08" FT METAL 276 FT /note="Magnesium 3" FT /evidence="ECO:0000250|UniProtKB:Q9UR08" FT METAL 280 FT /note="Magnesium 3" FT /evidence="ECO:0000250|UniProtKB:Q9UR08" FT BINDING 230 FT /note="Substrate" FT /evidence="ECO:0000250|UniProtKB:Q9UR08" FT BINDING 283 FT /note="Substrate" FT /evidence="ECO:0000250|UniProtKB:Q9UR08" SQ SEQUENCE 386 AA; 44939 MW; 063520D2A468FC5A CRC64; MGQPTTTSLF MRDVMFHRMT GTSQAVNDVA TLSGERREII RRALNKKILV PNILELMPAW PSEFQPNIDE VNVEIDEWLK TVNVAKEKKL KHRARGNYTL LAGIYYPHCR KEKMLALSQF LYWIFFWDDE IDTGGELTED REGTILCCAE TNKCINDCLG PEPNYTPPPG SRGTVEMLYP ILRDLRAGLS PVSTMRLKQE LHDYVNGVKN QQKVRQEDHL PNPWDHFQMR VDDVGVIPSI TQNEYAMDFT LPDWIRRHEA MEEIVLQCTK LTILLNEILS LQKEFRVSQL ENLCLLFMNT YDMSIEQSIH KVLGLLKDHY KICIEAEARL PWSTTDEKLN NNIREYIRGC QRLATGTACW SYNCERYFKL SQLNDQQELL LDLSRT //