TATC6_HYPAT
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 03-AUG-2022, entry version 10.
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 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"
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
