TPS3_MATCR
ID TPS3_MATCR Reviewed; 563 AA.
AC I6QSN0;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Germacrene-A synthase;
DE EC=4.2.3.23;
DE AltName: Full=Terpene synthase 3;
OS Matricaria chamomilla var. recutita (German chamomile) (Chamomilla
OS recutita).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC Matricariinae; Matricaria.
OX NCBI_TaxID=127986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Bodegold;
RX PubMed=22682202; DOI=10.1186/1471-2229-12-84;
RA Irmisch S., Krause S.T., Kunert G., Gershenzon J., Degenhardt J.,
RA Koellner T.G.;
RT "The organ-specific expression of terpene synthase genes contributes to the
RT terpene hydrocarbon composition of chamomile essential oils.";
RL BMC Plant Biol. 12:84-84(2012).
CC -!- FUNCTION: Sesquiterpene synthase involved in germacrene A biosynthesis.
CC May be involved in the biosynthesis of the sesquiterpene lactone
CC matricine, one of the major active compounds of chamomile flowers.
CC {ECO:0000269|PubMed:22682202}.
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:22682202};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- TISSUE SPECIFICITY: High expression in disk florets, moderate
CC expression in ray florets and detected in leaves and stems, but not in
CC roots. {ECO:0000269|PubMed:22682202}.
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. Tpsa subfamily.
CC {ECO:0000305}.
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DR EMBL; JQ255377; AFM43736.1; -; mRNA.
DR AlphaFoldDB; I6QSN0; -.
DR SMR; I6QSN0; -.
DR UniPathway; UPA00213; -.
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: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 Lyase; Magnesium; Manganese; Metal-binding.
FT CHAIN 1..563
FT /note="Germacrene-A synthase"
FT /id="PRO_0000421927"
FT MOTIF 316..320
FT /note="DDXXD motif"
FT BINDING 316
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 460
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 468
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 563 AA; 64871 MW; 6655A4C98ECEA785 CRC64;
MAAIQANVTT GIPANANTIT SSEPVRPLAN FPPSVWGDRF LSFSLDKSEL ERHAIAMEKP
KEDLRKLIVD PTMDSNEKLG LIYSVHRLGL TYMFMKEIES QLDKLFKEFS LQDCEEVDLY
TISINFQVFR HLGYKLPSDV FNKFKDASSG TFRESITRDV KGMLGLYESA QLRTRGEKVL
DEASVFIEGK LKSVVSTLEG NLAQQVKQSL RRPFHQGMPM IEARLYFSNY EEECSSHDSL
FKLAKLHFKY LELQQKEELR IVTKWWKDMR FQETTPYIRD RVPEIYLWIL GLYFEPRYSL
ARIIATKITL FLVVLDDTYD AYATIEEIRL LTDAINKWDI SAMEQIPEYI RPFYKILLDE
YAEIENIMAR EGRANTVIAS KEAFQDIARG YLEEAEWTNN GYVASFPEYM KNGLITSAYN
VISKSALVGM GEIVSEDALA WYESHLKTLQ ASELISRLQD DVMTYQFERE RGQSATGVDA
FIKTYGVSEK KAIDELKIMI ENAWKDINEG CLKPRQVSMD LLAPILNLAR MIDVVYRYDD
GFTFPGKTLK EYINLLFVGS LPM
