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 02-OCT-2024, entry version 15. 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 PDB; 7W5F; X-ray; 2.53 A; A/B=1-386. DR PDB; 7W5G; X-ray; 1.80 A; A=1-386. DR PDB; 7W5H; X-ray; 2.05 A; A/B=1-386. DR PDB; 7W5I; X-ray; 2.13 A; A/B=1-386. DR PDB; 7W5J; X-ray; 2.05 A; A/B=1-386. DR PDBsum; 7W5F; -. DR PDBsum; 7W5G; -. DR PDBsum; 7W5H; -. DR PDBsum; 7W5I; -. DR PDBsum; 7W5J; -. 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 GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProt. DR Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 1. DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf. DR InterPro; IPR034686; Terpene_cyclase-like_2. DR InterPro; IPR050225; Terpene_synthase. DR PANTHER; PTHR35201; TERPENE SYNTHASE; 1. DR PANTHER; PTHR35201:SF4; TERPENE SYNTHASE; 1. DR Pfam; PF19086; Terpene_syn_C_2; 1. DR SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1. DR SFLD; SFLDG01020; Terpene_Cyclase_Like_2; 1. DR SUPFAM; SSF48576; Terpenoid synthases; 1. PE 1: Evidence at protein level; KW 3D-structure; Lyase; Magnesium; Metal-binding. FT CHAIN 1..386 FT /note="Terpene cyclase 6" FT /id="PRO_0000452513" 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 BINDING 128 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q9UR08" FT BINDING 128 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q9UR08" FT BINDING 230 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q9UR08" FT BINDING 276 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:Q9UR08" FT BINDING 280 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:Q9UR08" FT BINDING 283 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q9UR08" FT BINDING 366..367 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q9UR08" FT HELIX 32..43 FT /evidence="ECO:0007829|PDB:7W5G" FT STRAND 47..50 FT /evidence="ECO:0007829|PDB:7W5G" FT HELIX 53..56 FT /evidence="ECO:0007829|PDB:7W5G" FT HELIX 68..79 FT /evidence="ECO:0007829|PDB:7W5G" FT STRAND 82..84 FT /evidence="ECO:0007829|PDB:7W5H" FT HELIX 86..95 FT /evidence="ECO:0007829|PDB:7W5G" FT HELIX 98..105 FT /evidence="ECO:0007829|PDB:7W5G" FT HELIX 111..131 FT /evidence="ECO:0007829|PDB:7W5G" FT TURN 136..139 FT /evidence="ECO:0007829|PDB:7W5G" FT HELIX 141..159 FT /evidence="ECO:0007829|PDB:7W5G" FT STRAND 160..162 FT /evidence="ECO:0007829|PDB:7W5G" FT HELIX 173..176 FT /evidence="ECO:0007829|PDB:7W5G" FT HELIX 178..186 FT /evidence="ECO:0007829|PDB:7W5G" FT HELIX 191..211 FT /evidence="ECO:0007829|PDB:7W5G" FT HELIX 223..233 FT /evidence="ECO:0007829|PDB:7W5G" FT HELIX 237..246 FT /evidence="ECO:0007829|PDB:7W5G" FT HELIX 253..256 FT /evidence="ECO:0007829|PDB:7W5G" FT HELIX 259..279 FT /evidence="ECO:0007829|PDB:7W5G" FT HELIX 281..286 FT /evidence="ECO:0007829|PDB:7W5G" FT HELIX 293..301 FT /evidence="ECO:0007829|PDB:7W5G" FT HELIX 305..327 FT /evidence="ECO:0007829|PDB:7W5G" FT HELIX 337..361 FT /evidence="ECO:0007829|PDB:7W5G" FT STRAND 364..368 FT /evidence="ECO:0007829|PDB:7W5G" FT HELIX 370..372 FT /evidence="ECO:0007829|PDB:7W5G" FT STRAND 379..382 FT /evidence="ECO:0007829|PDB:7W5G" 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 //