TPSD1_ABIGR
ID TPSD1_ABIGR Reviewed; 817 AA.
AC O81086; Q94FW2; Q9SAU6;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Alpha-bisabolene synthase;
DE EC=4.2.3.38 {ECO:0000269|PubMed:22153510, ECO:0000269|PubMed:9618485};
DE AltName: Full=(E)-alpha-bisabolene synthase;
DE AltName: Full=AgfEabis;
GN Name=ag1;
OS Abies grandis (Grand fir) (Pinus grandis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Abies.
OX NCBI_TaxID=46611;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND
RP INDUCTION.
RX PubMed=9618485; DOI=10.1073/pnas.95.12.6756;
RA Bohlmann J., Crock J., Jetter R., Croteau R.B.;
RT "Terpenoid-based defenses in conifers: cDNA cloning, characterization, and
RT functional expression of wound-inducible (E)-alpha-bisabolene synthase from
RT grand fir (Abies grandis).";
RL Proc. Natl. Acad. Sci. U.S.A. 95:6756-6761(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-817, AND NOMENCLATURE.
RX PubMed=11404343; DOI=10.1093/genetics/158.2.811;
RA Trapp S.C., Croteau R.B.;
RT "Genomic organization of plant terpene synthases and molecular evolutionary
RT implications.";
RL Genetics 158:811-832(2001).
RN [3]
RP GENE FAMILY, NOMENCLATURE, AND FUNCTION.
RX PubMed=9539701; DOI=10.1073/pnas.95.8.4126;
RA Bohlmann J., Meyer-Gauen G., Croteau R.B.;
RT "Plant terpenoid synthases: molecular biology and phylogenetic analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:4126-4133(1998).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF ASP-570 AND ASP-713.
RX PubMed=22153510; DOI=10.1016/j.str.2011.09.013;
RA McAndrew R.P., Peralta-Yahya P.P., DeGiovanni A., Pereira J.H., Hadi M.Z.,
RA Keasling J.D., Adams P.D.;
RT "Structure of a three-domain sesquiterpene synthase: a prospective target
RT for advanced biofuels production.";
RL Structure 19:1876-1884(2011).
CC -!- FUNCTION: Converts farnesyl diphosphate to alpha-bisabolene
CC (PubMed:9618485, PubMed:9539701, PubMed:22153510). Involved in
CC defensive oleoresin formation in conifers in response to insect attack
CC or other injury (PubMed:9618485, PubMed:9539701). Involved in
CC sesquiterpene (C15) olefins biosynthesis (PubMed:9618485,
CC PubMed:9539701). {ECO:0000269|PubMed:22153510,
CC ECO:0000269|PubMed:9539701, ECO:0000269|PubMed:9618485}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (E,R)-alpha-bisabolene +
CC diphosphate; Xref=Rhea:RHEA:25436, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:49243, ChEBI:CHEBI:175763; EC=4.2.3.38;
CC Evidence={ECO:0000269|PubMed:22153510, ECO:0000269|PubMed:9618485};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:22153510, ECO:0000269|PubMed:9618485};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:9618485};
CC Note=Binds 3 divalent metal cations per subunit (PubMed:22153510). Can
CC use either Mg(2+) or Mn(2+) (PubMed:9618485).
CC {ECO:0000269|PubMed:22153510, ECO:0000269|PubMed:9618485};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=49.5 uM for (2E,6E)-farnesyl diphosphate
CC {ECO:0000269|PubMed:22153510};
CC -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: By wounding. {ECO:0000269|PubMed:9618485}.
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 -!- MISCELLANEOUS: The conserved 25-Arg-Arg-26 motif may play a role in the
CC isomerization step of the terpenoid cyclization reaction sequence.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily.
CC {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; AF006195; AAC24192.1; -; mRNA.
DR EMBL; AF006194; AAC24191.1; -; mRNA.
DR EMBL; AF326515; AAK83562.1; -; Genomic_DNA.
DR PDB; 3SAE; X-ray; 1.96 A; A=1-817.
DR PDB; 3SDQ; X-ray; 2.14 A; A=1-817.
DR PDB; 3SDR; X-ray; 1.86 A; A=1-817.
DR PDB; 3SDT; X-ray; 1.89 A; A=1-817.
DR PDB; 3SDU; X-ray; 1.89 A; A=1-817.
DR PDB; 3SDV; X-ray; 2.20 A; A=1-817.
DR PDBsum; 3SAE; -.
DR PDBsum; 3SDQ; -.
DR PDBsum; 3SDR; -.
DR PDBsum; 3SDT; -.
DR PDBsum; 3SDU; -.
DR PDBsum; 3SDV; -.
DR AlphaFoldDB; O81086; -.
DR SMR; O81086; -.
DR PRIDE; O81086; -.
DR KEGG; ag:AAC24192; -.
DR BRENDA; 4.2.3.38; 2.
DR UniPathway; UPA00924; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0052681; F:alpha-bisabolene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
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; 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 SUPFAM; SSF48239; SSF48239; 2.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lyase; Magnesium; Manganese; Metal-binding.
FT CHAIN 1..817
FT /note="Alpha-bisabolene synthase"
FT /id="PRO_0000186446"
FT MOTIF 566..570
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 566
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22153510,
FT ECO:0007744|PDB:3SAE, ECO:0007744|PDB:3SDU"
FT BINDING 566
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:22153510,
FT ECO:0007744|PDB:3SAE, ECO:0007744|PDB:3SDU"
FT BINDING 570
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22153510,
FT ECO:0007744|PDB:3SAE, ECO:0007744|PDB:3SDU"
FT BINDING 570
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:22153510,
FT ECO:0007744|PDB:3SAE, ECO:0007744|PDB:3SDU"
FT BINDING 713
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:22153510,
FT ECO:0007744|PDB:3SAE, ECO:0007744|PDB:3SDU"
FT BINDING 717
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:22153510,
FT ECO:0007744|PDB:3SAE, ECO:0007744|PDB:3SDU"
FT BINDING 721
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:22153510,
FT ECO:0007744|PDB:3SAE, ECO:0007744|PDB:3SDU"
FT MUTAGEN 570
FT /note="D->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:22153510"
FT MUTAGEN 713
FT /note="D->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:22153510"
FT CONFLICT 65
FT /note="A -> V (in Ref. 1; AAC24191 and 2; AAK83562)"
FT /evidence="ECO:0000305"
FT CONFLICT 590
FT /note="L -> V (in Ref. 2; AAK83562)"
FT /evidence="ECO:0000305"
FT CONFLICT 655
FT /note="T -> S (in Ref. 2; AAK83562)"
FT /evidence="ECO:0000305"
FT CONFLICT 784
FT /note="R -> G (in Ref. 2; AAK83562)"
FT /evidence="ECO:0000305"
FT HELIX 36..41
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 50..71
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:3SDR"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 104..112
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 128..144
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 149..163
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 179..192
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 202..216
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 229..236
FT /evidence="ECO:0007829|PDB:3SDR"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:3SDR"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 260..270
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 273..286
FT /evidence="ECO:0007829|PDB:3SDR"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 297..310
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 318..331
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 348..360
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 367..373
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 387..401
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 409..426
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 429..432
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 434..438
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 441..450
FT /evidence="ECO:0007829|PDB:3SDR"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:3SDQ"
FT HELIX 458..466
FT /evidence="ECO:0007829|PDB:3SDR"
FT STRAND 475..481
FT /evidence="ECO:0007829|PDB:3SDR"
FT TURN 484..486
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 489..519
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 522..524
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 532..540
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 546..548
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 549..570
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 575..587
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 590..595
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 598..622
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 627..649
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 656..666
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 669..677
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 687..691
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 701..716
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 730..737
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 743..766
FT /evidence="ECO:0007829|PDB:3SDR"
FT STRAND 769..771
FT /evidence="ECO:0007829|PDB:3SDT"
FT HELIX 773..789
FT /evidence="ECO:0007829|PDB:3SDR"
FT HELIX 800..811
FT /evidence="ECO:0007829|PDB:3SDR"
SQ SEQUENCE 817 AA; 93749 MW; 95FB06DBC0DE1B4B CRC64;
MAGVSAVSKV SSLVCDLSST SGLIRRTANP HPNVWGYDLV HSLKSPYIDS SYRERAEVLV
SEIKAMLNPA ITGDGESMIT PSAYDTAWVA RVPAIDGSAR PQFPQTVDWI LKNQLKDGSW
GIQSHFLLSD RLLATLSCVL VLLKWNVGDL QVEQGIEFIK SNLELVKDET DQDSLVTDFE
IIFPSLLREA QSLRLGLPYD LPYIHLLQTK RQERLAKLSR EEIYAVPSPL LYSLEGIQDI
VEWERIMEVQ SQDGSFLSSP ASTACVFMHT GDAKCLEFLN SVMIKFGNFV PCLYPVDLLE
RLLIVDNIVR LGIYRHFEKE IKEALDYVYR HWNERGIGWG RLNPIADLET TALGFRLLRL
HRYNVSPAIF DNFKDANGKF ICSTGQFNKD VASMLNLYRA SQLAFPGENI LDEAKSFATK
YLREALEKSE TSSAWNNKQN LSQEIKYALK TSWHASVPRV EAKRYCQVYR PDYARIAKCV
YKLPYVNNEK FLELGKLDFN IIQSIHQEEM KNVTSWFRDS GLPLFTFARE RPLEFYFLVA
AGTYEPQYAK CRFLFTKVAC LQTVLDDMYD TYGTLDELKL FTEAVRRWDL SFTENLPDYM
KLCYQIYYDI VHEVAWEAEK EQGRELVSFF RKGWEDYLLG YYEEAEWLAA EYVPTLDEYI
KNGITSIGQR ILLLSGVLIM DGQLLSQEAL EKVDYPGRRV LTELNSLISR LADDTKTYKA
EKARGELASS IECYMKDHPE CTEEEALDHI YSILEPAVKE LTREFLKPDD VPFACKKMLF
EETRVTMVIF KDGDGFGVSK LEVKDHIKEC LIEPLPL
