VTSS1_HYOMU
ID VTSS1_HYOMU Reviewed; 555 AA.
AC Q39978;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Vetispiradiene synthase 1;
DE Short=HVS1;
DE EC=4.2.3.21;
OS Hyoscyamus muticus (Egyptian henbane).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Hyoscyameae;
OC Hyoscyamus.
OX NCBI_TaxID=35626;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 36-555, CATALYTIC ACTIVITY, AND INDUCTION BY
RP ELICITOR.
RX PubMed=7706281; DOI=10.1074/jbc.270.13.7375;
RA Back K., Chappell J.;
RT "Cloning and bacterial expression of a sesquiterpene cyclase from
RT Hyoscyamus muticus and its molecular comparison to related terpene
RT cyclases.";
RL J. Biol. Chem. 270:7375-7381(1995).
RN [2]
RP CONCEPTUAL TRANSLATION.
RA Chappell J.;
RL Unpublished observations (JAN-1995).
CC -!- FUNCTION: Sesquiterpene synthase that catalyzes the formation of
CC vetispiradiene from trans,trans-farnesyl diphosphate. The initial
CC internal cyclization produces the monocyclic intermediate germacrene A.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (-)-vetispiradiene +
CC diphosphate; Xref=Rhea:RHEA:10340, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:46971, ChEBI:CHEBI:175763; EC=4.2.3.21;
CC Evidence={ECO:0000269|PubMed:7706281};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: By elicitor from R.solani. {ECO:0000269|PubMed:7706281}.
CC -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for
CC the catalytic activity, presumably through binding to Mg(2+).
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC {ECO:0000305}.
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DR EMBL; U20188; AAA86337.1; -; mRNA.
DR PIR; A56118; A56118.
DR PDB; 5JO7; X-ray; 2.15 A; A/B/C/D=23-555.
DR PDBsum; 5JO7; -.
DR AlphaFoldDB; Q39978; -.
DR SMR; Q39978; -.
DR KEGG; ag:AAA86337; -.
DR BioCyc; MetaCyc:VS1-MON; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0034003; F:vetispiradiene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR CDD; cd00684; Terpene_cyclase_plant_C1; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR Gene3D; 1.50.10.130; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR034741; Terpene_cyclase-like_1_C.
DR InterPro; IPR044814; Terpene_cyclase_plant_C1.
DR InterPro; IPR001906; Terpene_synth_N.
DR InterPro; IPR036965; Terpene_synth_N_sf.
DR InterPro; IPR005630; Terpene_synthase_metal-bd.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR Pfam; PF01397; Terpene_synth; 1.
DR Pfam; PF03936; Terpene_synth_C; 1.
DR SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lyase; Magnesium; Metal-binding.
FT CHAIN 1..555
FT /note="Vetispiradiene synthase 1"
FT /id="PRO_0000398184"
FT MOTIF 308..312
FT /note="DDXXD motif"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 451
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 455
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 459
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT HELIX 38..60
FT /evidence="ECO:0007829|PDB:5JO7"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:5JO7"
FT HELIX 67..79
FT /evidence="ECO:0007829|PDB:5JO7"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:5JO7"
FT HELIX 87..100
FT /evidence="ECO:0007829|PDB:5JO7"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:5JO7"
FT HELIX 112..124
FT /evidence="ECO:0007829|PDB:5JO7"
FT HELIX 131..137
FT /evidence="ECO:0007829|PDB:5JO7"
FT HELIX 146..150
FT /evidence="ECO:0007829|PDB:5JO7"
FT HELIX 152..162
FT /evidence="ECO:0007829|PDB:5JO7"
FT HELIX 170..186
FT /evidence="ECO:0007829|PDB:5JO7"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:5JO7"
FT HELIX 194..203
FT /evidence="ECO:0007829|PDB:5JO7"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:5JO7"
FT HELIX 211..224
FT /evidence="ECO:0007829|PDB:5JO7"
FT HELIX 230..261
FT /evidence="ECO:0007829|PDB:5JO7"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:5JO7"
FT HELIX 274..284
FT /evidence="ECO:0007829|PDB:5JO7"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:5JO7"
FT HELIX 291..312
FT /evidence="ECO:0007829|PDB:5JO7"
FT HELIX 317..329
FT /evidence="ECO:0007829|PDB:5JO7"
FT HELIX 332..337
FT /evidence="ECO:0007829|PDB:5JO7"
FT HELIX 340..361
FT /evidence="ECO:0007829|PDB:5JO7"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:5JO7"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:5JO7"
FT HELIX 369..392
FT /evidence="ECO:0007829|PDB:5JO7"
FT HELIX 398..405
FT /evidence="ECO:0007829|PDB:5JO7"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:5JO7"
FT HELIX 411..417
FT /evidence="ECO:0007829|PDB:5JO7"
FT TURN 418..421
FT /evidence="ECO:0007829|PDB:5JO7"
FT HELIX 427..434
FT /evidence="ECO:0007829|PDB:5JO7"
FT HELIX 438..459
FT /evidence="ECO:0007829|PDB:5JO7"
FT STRAND 461..465
FT /evidence="ECO:0007829|PDB:5JO7"
FT HELIX 468..476
FT /evidence="ECO:0007829|PDB:5JO7"
FT HELIX 480..501
FT /evidence="ECO:0007829|PDB:5JO7"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:5JO7"
FT HELIX 510..526
FT /evidence="ECO:0007829|PDB:5JO7"
FT HELIX 542..549
FT /evidence="ECO:0007829|PDB:5JO7"
SQ SEQUENCE 555 AA; 64317 MW; 5C61576933E89D41 CRC64;
MAPAIVMSNY EEEEIVRPVA DFSPSLWGDH FHSFSVDNQV AEKYAQEIET LKEQTSTMLS
AACGTTLTEK LNLIDIIERL GIAYHFEKQI EDMLDHIYRA DPYFEAHEYN DLNTSSVQFR
LLRQHGYNVS PNIFSRFQDA NGKFKESLRS DIRGLLNLYE ASHVRTHKED ILEEALVFSV
GHLESAAPHL KSPLSKQVTH ALEQSLHKSI PRVEIRYFIS IYEEEEFKND LLLRFAKLDY
NLLQMLHKHE LSEVSRWWKD LDFVTTLPYA RDRAVECYFW TMGVYAEPQY SQARVMLAKT
IAMISIVDDT FDAYGIVKEL EVYTDAIQRW DISQIDRLPE YMKISYKALL DLYDDYEKEL
SKDGRSDVVH YAKERMKEIV GNYFIEGKWF IEGYMPSVSE YLSNALATST YYLLTTTSYL
GMKSATKEHF EWLATNPKIL EANATLCRVV DDIATYEVEK GRGQIATGIE CYMRDYGVST
EVAMEKFQEM ADIAWKDVNE EILRPTPVSS EILTRILNLA RIIDVTYKHN QDGYTHPEKV
LKPHIIALVV DSIDI
