GASS_CICIN
ID GASS_CICIN Reviewed; 558 AA.
AC Q8LSC2;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Germacrene A synthase short form;
DE Short=CiGASsh;
DE EC=4.2.3.23;
OS Cichorium intybus (Chicory).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Cichorioideae; Cichorieae;
OC Cichoriinae; Cichorium.
OX NCBI_TaxID=13427;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12011345; DOI=10.1104/pp.001024;
RA Bouwmeester H.J., Kodde J., Verstappen F.W., Altug I.G., de Kraker J.W.,
RA Wallaart T.E.;
RT "Isolation and characterization of two germacrene A synthase cDNA clones
RT from chicory.";
RL Plant Physiol. 129:134-144(2002).
CC -!- FUNCTION: Involved in sesquiterpene lactone biosynthesis. Produces
CC exclusively (+)-germacrene A. {ECO:0000269|PubMed:12011345}.
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:12011345};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.2 uM for 2-trans,6-trans-farnesyl diphosphate
CC {ECO:0000269|PubMed:12011345};
CC Vmax=21.5 pmol/h/mg enzyme {ECO:0000269|PubMed:12011345};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:12011345};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- TISSUE SPECIFICITY: Expressed in roots and in green and etiolated
CC seedlings. {ECO:0000269|PubMed:12011345}.
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 -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; AF498000; AAM21659.1; -; mRNA.
DR AlphaFoldDB; Q8LSC2; -.
DR SMR; Q8LSC2; -.
DR PRIDE; Q8LSC2; -.
DR KEGG; ag:AAM21659; -.
DR BioCyc; MetaCyc:MON-13557; -.
DR BRENDA; 4.2.3.23; 1385.
DR UniPathway; UPA00213; -.
DR GO; GO:0034005; F:germacrene-A synthase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0045338; P:farnesyl diphosphate metabolic 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 Lyase; Magnesium; Metal-binding.
FT CHAIN 1..558
FT /note="Germacrene A synthase short form"
FT /id="PRO_0000398154"
FT MOTIF 311..315
FT /note="DDXXD motif"
FT BINDING 311
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 311
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 315
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 315
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 455
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 459
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 558 AA; 64383 MW; 25280F662D625FC6 CRC64;
MAAVEANGTF QANTKTTEPV RPLANFPPSV WGDRFLSFSL DTTELEGYAK AMEEPKEEVR
KLIVDPTMDS NKKLSLIYSV HRLGLTYLFL QEIEAQLDKL FKEFNLQDYD EFDLYTTSIN
FQVFRHLGHK LPCDVFNKFK DSSSGTFKES ITNDVKGMLG LYESAQLRLR GEPILDEASA
FTETQLKSVV NTLEGNLAKQ VMQSLRRPFH QGMPMVEARM YFSNYDEECS THESLPKLAK
LHFNYLQLQQ KEELRIVSKW WKDMRFQETT PYIRDRVPEI YLWILGLYFE PRYSLARIIA
TKITLFLVVL DDTYDAYATI EEIRLLTDAI NRWDISAMEQ IPEYIRPFYK ILLDEYAELE
KQLAKEGRAK SVIASKEAFQ DIARGYLEEA EWTNSGYVAS FPEYMKNGLI TSAYNVISKS
ALVGMGEMVG EDALAWYESH PKTLQASELI SRLQDDVMTY QFERERGQSA TGVDSYIKTY
GVTEKEAIDE LNKMIENAWK DINEGCLKPR EVSMDLLAPI LNLARMIDVV YRYDDGFTFP
GKTMKEYITL LFVGSSPM
