GASL_CICIN
ID GASL_CICIN Reviewed; 583 AA.
AC Q8LSC3;
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 long form;
DE Short=CiGASlo;
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).
RN [2]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9701594; DOI=10.1104/pp.117.4.1381;
RA de Kraker J.W., Franssen M.C., de Groot A., Konig W.A., Bouwmeester H.J.;
RT "(+)-Germacrene A biosynthesis. The committed step in the biosynthesis of
RT bitter sesquiterpene lactones in chicory.";
RL Plant Physiol. 117:1381-1392(1998).
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, ECO:0000269|PubMed:9701594};
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=6.9 uM for 2-trans,6-trans-farnesyl diphosphate
CC {ECO:0000269|PubMed:12011345, ECO:0000269|PubMed:9701594};
CC Vmax=13.9 pmol/h/mg enzyme {ECO:0000269|PubMed:12011345,
CC ECO:0000269|PubMed:9701594};
CC pH dependence:
CC Optimum pH is 6.8. {ECO:0000269|PubMed:12011345,
CC ECO:0000269|PubMed:9701594};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- TISSUE SPECIFICITY: Expressed in roots, in head core tissue and leaves,
CC in green and etiolated seedlings, and at a much lower level in green
CC leaves. {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; AF497999; AAM21658.1; -; mRNA.
DR AlphaFoldDB; Q8LSC3; -.
DR SMR; Q8LSC3; -.
DR PRIDE; Q8LSC3; -.
DR KEGG; ag:AAM21658; -.
DR BioCyc; MetaCyc:MON-13558; -.
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..583
FT /note="Germacrene A synthase long form"
FT /id="PRO_0000398153"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 333..337
FT /note="DDXXD motif"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 333
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 333
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 477
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 481
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 485
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 583 AA; 67075 MW; 2A4E6A82B7BE8F8C CRC64;
MALVRNNSSN GREPVLSPRS LTSPRGLTSP RPLSVQPTPE PVRPLANFPP SIWADRFISF
SLDNSQLEAY ANALEEPKEA VKSLITDTTI DANTKLKLIY SVHRLGLSYL YPDEIDAELN
KLFEKIDLQY YEQVDLYTIA VQFQVFRHHG YKISSDVFKK FKDSTTGTFT DDVTKDVKGM
LSLYESAHLR LHGEDILDEA LAFTEAHLKK ILTTLEGDLA RQVNQVLKRP FHTGMPMVEA
RLYFITHEED FSSHESVVKL AKVHFNYLQL QQKEELRLVS QWWKDMQFQQ SVPYIRDRVP
EIYLWILGLY FEPYYSRARI IATKITLFLV VLDDTYDAYA TIDEIRSITD AINRWEISAI
DQLPEYIKPF YRILLNEYDD LEKEYSKDGR AFSVHASKQA FQEIARGYLE EAEWLHNGYV
ATFPEYMKNG LITSAYNVIS KSALVGMGAI ADEEALAWYE THPKILKASE LISRLQDDVM
TFQFERKRGQ SATGVDAYIK EYNVSEEVAI KELMKMIENA WKDINEGCLK PTEVSVALLT
PILNLARMID VVYKFDDGFT FPGKTLKDYI TLLFVSPPPS LEN
