ID   TPSGB_SOLHA             Reviewed;         544 AA.
AC   Q9FQ27;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=(E,E)-germacrene B synthase;
DE            EC=4.2.3.71;
GN   Name=SSTLH1;
OS   Solanum habrochaites (Wild tomato) (Lycopersicon hirsutum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=62890;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=11090225; DOI=10.1105/tpc.12.11.2283;
RA   van Der Hoeven R.S., Monforte A.J., Breeden D., Tanksley S.D.,
RA   Steffens J.C.;
RT   "Genetic Control and Evolution of Sesquiterpene Biosynthesis in
RT   Lycopersicon esculentum and Lycopersicon hirsutum.";
RL   Plant Cell 12:2283-2294(2000).
CC   -!- FUNCTION: Involved in the biosynthesis of germacrene B.
CC       {ECO:0000269|PubMed:11090225}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = (1E,4E)-germacrene B +
CC         diphosphate; Xref=Rhea:RHEA:25444, ChEBI:CHEBI:5337,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.71;
CC         Evidence={ECO:0000269|PubMed:11090225};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305};
CC       Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000305};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; AF279455; AAG41891.1; -; mRNA.
DR   AlphaFoldDB; Q9FQ27; -.
DR   SMR; Q9FQ27; -.
DR   KEGG; ag:AAG41891; -.
DR   BRENDA; 4.2.3.71; 3102.
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: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; Manganese; Metal-binding.
FT   CHAIN           1..544
FT                   /note="(E,E)-germacrene B synthase"
FT                   /id="PRO_0000412240"
FT   MOTIF           296..300
FT                   /note="DDXXD motif"
FT   BINDING         296
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         296
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         300
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         300
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         449
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   544 AA;  63723 MW;  16EA14FCDEA048BB CRC64;
     MAASSANKSR PLANFHPTVW GYHFLSYTHE ITNQEKVEVD EYKETIRKML VEAPEGSEQK
     LVLIDAMQRL GVAYHFHNEI ETSIQNIFDA PKQNNNLHIV SLRFRLVRQQ GHYMSSDVFK
     QFTNQDGKFK ETLTNDVQGL LSLYEASYLR VRDEEILEEA LAFTTTHLKS IVSTMSNNNN
     SLKVEVSEAL TQPIRMTLPR MEARRYISIY ENNDAHNHLL LKFAKLDFNM LQKLHQRELS
     DLTRWWKDLD FANKYPYARD RLVECYFWIL GVYFEPKYSR ARKMMTKVLK MTSIIDDTFD
     AYATFDELEP FNDAIQRWDA NAIDSIPPYM RPAYQAFLDI YSEMEQVLSK KGKLDRVYYA
     KNEMKKLVRA YFKETQWLND CDHIPKYEEH MENSLVSGGY MMIPTTCLVG MEEFISIETF
     EWLMNDPLIV RASSLIARAM NDIVGHEVEQ ERGHVASLIE CYMKDYGASK QEAYAKFKKD
     VTNAWKDINK EFFRPTEVPM FVLERVLNLT RAAEPLYKEK DAYTNAKGKL KNMINSILIE
     SVKI