ID   TPSCS_POGCB             Reviewed;         545 AA.
AC   Q49SP7;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Gamma-curcumene synthase;
DE            EC=4.2.3.94;
DE   AltName: Full=PatTpsA;
OS   Pogostemon cablin (Patchouli) (Mentha cablin).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lamiaceae; Lamioideae; Pogostemoneae;
OC   Pogostemon.
OX   NCBI_TaxID=28511;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=16970904; DOI=10.1016/j.abb.2006.08.006;
RA   Deguerry F., Pastore L., Wu S., Clark A., Chappell J., Schalk M.;
RT   "The diverse sesquiterpene profile of patchouli, Pogostemon cablin, is
RT   correlated with a limited number of sesquiterpene synthases.";
RL   Arch. Biochem. Biophys. 454:123-136(2006).
CC   -!- FUNCTION: Sesquiterpene synthase involved in gamma-curcumene
CC       biosynthesis. {ECO:0000269|PubMed:16970904}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + gamma-curcumene;
CC         Xref=Rhea:RHEA:32031, ChEBI:CHEBI:33019, ChEBI:CHEBI:63696,
CC         ChEBI:CHEBI:175763; EC=4.2.3.94;
CC         Evidence={ECO:0000269|PubMed:16970904};
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, cytosol {ECO:0000250}.
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; AY508726; AAS86319.1; -; mRNA.
DR   AlphaFoldDB; Q49SP7; -.
DR   SMR; Q49SP7; -.
DR   KEGG; ag:AAS86319; -.
DR   BioCyc; MetaCyc:MON-14858; -.
DR   BRENDA; 4.2.3.94; 9724.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0102064; F:gamma-curcumene synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0010334; F:sesquiterpene synthase activity; IDA:UniProtKB.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR   GO; GO:0045338; P:farnesyl diphosphate metabolic process; IDA:UniProtKB.
DR   GO; GO:0051762; P:sesquiterpene biosynthetic process; IDA:UniProtKB.
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..545
FT                   /note="Gamma-curcumene synthase"
FT                   /id="PRO_0000419749"
FT   MOTIF           299..303
FT                   /note="DDXXD motif"
FT   BINDING         299
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         299
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         303
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         303
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         442
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         450
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   545 AA;  63586 MW;  E578CEC0DE21FB6E CRC64;
     MAAFTANAVD MRPPVITIHP RSKDIFSQFS LDDKLQKQYA QGIEALKEEA RSMLMAAKSA
     KVMILIDTLE RLGLGYHFEK EIEEKLEAIY KKEDGDDYDL FTTALRFRLL RQHQRRVPCS
     VFDKFMNKEG KFEEEPLISD VEGLLSLYDA AYLQIHGEHI LQEALIFTTH HLTRIEPQLD
     DHSPLKLKLN RALEFPFYRE IPIIYAHFYI SVYERDDSRD EVLLKMAKLS YNFLQNLYKK
     ELSQLSRWWN KLELIPNLPY IRDSVAGAYL WAVALYFEPQ YSDVRMAIAK LIQIAAAVDD
     TYDNYATIRE AQLLTEALER LNVHEIDTLP DYMKIVYRFV MSWSEDFERD ATIKEQMLAT
     PYFKAEMKKL GRAYNQELKW VMERQLPSFE EYMKNSEITS GVYIMFTVIS PYLNSATQKN
     IDWLLSQPRL ASSTAIVMRC CNDLGSNQRE SKGGEVMTSL DCYMKQHGAS KQETISKFKL
     IIEDEWKNLN EEWAATTCLP KVMVEIFRNY ARIAGFCYKN NGDAYTSPKI VQQCFDALFV
     NPLRI