ID   TPGAS_POGCB             Reviewed;         554 AA.
AC   Q49SP5;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Germacrene A synthase;
DE            EC=4.2.3.23;
DE   AltName: Full=PatTpsCF2;
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 germacrene A biosynthesis.
CC       Produces also dditional sesquiterpene products, including 4,5-di-epi-
CC       aristolochene, eremophilene, alpha-selinene.
CC       {ECO:0000269|PubMed:16970904}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = (+)-(R)-germacrene A +
CC         diphosphate; Xref=Rhea:RHEA:12516, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:41595, ChEBI:CHEBI:175763; EC=4.2.3.23;
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; AY508728; AAS86321.1; -; mRNA.
DR   AlphaFoldDB; Q49SP5; -.
DR   SMR; Q49SP5; -.
DR   BioCyc; MetaCyc:MON-14837; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0034005; F:germacrene-A 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..554
FT                   /note="Germacrene A synthase"
FT                   /id="PRO_0000419750"
FT   MOTIF           306..310
FT                   /note="DDXXD motif"
FT   BINDING         306
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         306
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         310
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         310
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         453
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         457
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   554 AA;  64232 MW;  42EFF9E433F2F223 CRC64;
     MAVQISETVR PFANFSPNPS LWGDQFINHK SKTQQISRIY LEEIEGLKNE VKCMLTSTPE
     GKMADTVNLI DTLERLGVSY HFEKEIEEKM KHLFNLIKAD NYKDHEGCDL YTDALHFRLF
     RQHGYPISSG IFNKWMDGNG KFKESIKSDA KGLLSLYEAC CLRTHGDTLL DEALVFATAS
     LKSMAANLAS PLRKQVEHAL FQHLHFGIPR VEARHFITFY EEEEHKNEML LRFAKLDFNA
     LQALHKEELS EISKWWKDLD LISKLPYARD RVVESYFWAV GVYYQPKYSR ARIMLTKTIA
     MTAILDDTYD SYGTLEELDV LTKAIERWDI KEINGLPEYI KGFYKQVLKL YQQLEEELAK
     EGRSYAVYYA IEACKELARS YAVEAKWFKK GYLPGFEEYL INSLVTSTAG YLNIISFFGV
     ESVTKEDFEW FSKKPRIAVA TQIITRVIDD IATYEVEKEK GQSATGIDCY MKEHGVSKEK
     AMQRFYEMST NAWKDINEEG LSWPSSFSRD IFVQLRNFSR MVDVTYGKNE DGYSKPEKIL
     KPLIIALFVD QIKL