TPSD5_ABIGR
ID TPSD5_ABIGR Reviewed; 593 AA.
AC O64405;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Gamma-humulene synthase;
DE EC=4.2.3.56;
DE AltName: Full=Agfghum;
GN Name=ag5;
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, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9442047; DOI=10.1074/jbc.273.4.2078;
RA Steele C.L., Crock J., Bohlmann J., Croteau R.B.;
RT "Sesquiterpene synthases from grand fir (Abies grandis). Comparison of
RT constitutive and wound-induced activities, and cDNA isolation,
RT characterization, and bacterial expression of delta-selinene synthase and
RT gamma-humulene synthase.";
RL J. Biol. Chem. 273:2078-2089(1998).
RN [2]
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 [3]
RP GENE FAMILY, NOMENCLATURE, AND FUNCTION.
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).
CC -!- FUNCTION: Involved in defensive oleoresin formation in conifers in
CC response to insect attack or other injury. Involved in 52 sesquiterpene
CC (C15) olefins biosynthesis. {ECO:0000269|PubMed:11404343,
CC ECO:0000269|PubMed:9442047, ECO:0000269|PubMed:9539701}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + gamma-humulene;
CC Xref=Rhea:RHEA:25456, ChEBI:CHEBI:33019, ChEBI:CHEBI:49290,
CC ChEBI:CHEBI:175763; EC=4.2.3.56;
CC Evidence={ECO:0000269|PubMed:9442047};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + sibirene;
CC Xref=Rhea:RHEA:25460, ChEBI:CHEBI:33019, ChEBI:CHEBI:49231,
CC ChEBI:CHEBI:175763; EC=4.2.3.56;
CC Evidence={ECO:0000269|PubMed:9442047};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + longifolene;
CC Xref=Rhea:RHEA:25464, ChEBI:CHEBI:6530, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:175763; EC=4.2.3.56;
CC Evidence={ECO:0000269|PubMed:9442047};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = beta-himachalene + diphosphate;
CC Xref=Rhea:RHEA:25468, ChEBI:CHEBI:33019, ChEBI:CHEBI:49210,
CC ChEBI:CHEBI:175763; EC=4.2.3.56;
CC Evidence={ECO:0000269|PubMed:9442047};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + gamma-
CC himachalene; Xref=Rhea:RHEA:25472, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:49224, ChEBI:CHEBI:175763; EC=4.2.3.56;
CC Evidence={ECO:0000269|PubMed:9442047};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = alpha-himachalene +
CC diphosphate; Xref=Rhea:RHEA:25476, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:49214, ChEBI:CHEBI:175763; EC=4.2.3.56;
CC Evidence={ECO:0000269|PubMed:9442047};
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 -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.5 uM for farnesyl diphosphate {ECO:0000269|PubMed:9442047};
CC -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Constitutive expression.
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: In sesquiterpene synthases utilizing farnesyl
CC diphosphate as substrate, magnesium is more efficient as cofactor than
CC is manganese.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily.
CC {ECO:0000305}.
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DR EMBL; U92267; AAC05728.1; -; mRNA.
DR AlphaFoldDB; O64405; -.
DR SMR; O64405; -.
DR PRIDE; O64405; -.
DR KEGG; ag:AAC05728; -.
DR BioCyc; MetaCyc:AG5-MON; -.
DR BRENDA; 4.2.3.56; 2.
DR SABIO-RK; O64405; -.
DR UniPathway; UPA00924; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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 Cytoplasm; Lyase; Magnesium; Metal-binding.
FT CHAIN 1..593
FT /note="Gamma-humulene synthase"
FT /id="PRO_0000186448"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 343..347
FT /note="DDXXD motif"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 343
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 488
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 496
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 593 AA; 67937 MW; 632E9EF069F21BD4 CRC64;
MAQISESVSP STDLKSTESS ITSNRHGNMW EDDRIQSLNS PYGAPAYQER SEKLIEEIKL
LFLSDMDDSC NDSDRDLIKR LEIVDTVECL GIDRHFQPEI KLALDYVYRC WNERGIGEGS
RDSLKKDLNA TALGFRALRL HRYNVSSGVL ENFRDDNGQF FCGSTVEEEG AEAYNKHVRC
MLSLSRASNI LFPGEKVMEE AKAFTTNYLK KVLAGREATH VDESLLGEVK YALEFPWHCS
VQRWEARSFI EIFGQIDSEL KSNLSKKMLE LAKLDFNILQ CTHQKELQII SRWFADSSIA
SLNFYRKCYV EFYFWMAAAI SEPEFSGSRV AFTKIAILMT MLDDLYDTHG TLDQLKIFTE
GVRRWDVSLV EGLPDFMKIA FEFWLKTSNE LIAEAVKAQG QDMAAYIRKN AWERYLEAYL
QDAEWIATGH VPTFDEYLNN GTPNTGMCVL NLIPLLLMGE HLPIDILEQI FLPSRFHHLI
ELASRLVDDA RDFQAEKDHG DLSCIECYLK DHPESTVEDA LNHVNGLLGN CLLEMNWKFL
KKQDSVPLSC KKYSFHVLAR SIQFMYNQGD GFSISNKVIK DQVQKVLIVP VPI
