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Epi-cedrol synthase (EC 4.2.3.39) (8-epicedrol synthase)

 ECS1_ARTAN              Reviewed;         547 AA.
Q9LLR9; Q9ST45;
28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 63.
RecName: Full=Epi-cedrol synthase;
EC=4.2.3.39;
AltName: Full=8-epicedrol synthase;
Name=ECS1;
Artemisia annua (Sweet wormwood).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; asterids; campanulids; Asterales; Asteraceae;
Asteroideae; Anthemideae; Artemisiinae; Artemisia.
NCBI_TaxID=35608;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
PubMed=10486139; DOI=10.1006/abbi.1999.1357;
Hua L., Matsuda S.P.;
"The molecular cloning of 8-epicedrol synthase from Artemisia annua.";
Arch. Biochem. Biophys. 369:208-212(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND BIOPHYSICOCHEMICAL PROPERTIES.
TISSUE=Leaf;
PubMed=10486140; DOI=10.1006/abbi.1999.1358;
Mercke P., Xue Z.T., Brodelius P.E.;
"Cloning, expression, and characterization of epi-cedrol synthase, a
sesquiterpene cyclase from Artemisia annua L.";
Arch. Biochem. Biophys. 369:213-222(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=10996256; DOI=10.1016/S0168-9452(00)00322-8;
Van Geldre E., De Pauw I., Inze D., Van Montagu M.,
Van den Eeckhout E.;
"Cloning and molecular analysis of two new sesquiterpene cyclases from
Artemisia annua L.";
Plant Sci. 158:163-171(2000).
-!- FUNCTION: Sesquiterpene cyclase catalyzing the production of 8-
epi-cedrol. Able to convert geranyl diphosphate to monoterpens.
Can use farnesyl diphosphate or geranyl diphosphate as substrates,
but not geranylgeranyl diphosphate. Probably not involved in
artemisinin biosynthesis. {ECO:0000269|PubMed:10486139}.
-!- CATALYTIC ACTIVITY: (2E,6E)-farnesyl diphosphate + H(2)O = 8-epi-
cedrol + diphosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
-!- ENZYME REGULATION: Inhibited by high concentration of manganese.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.4 uM for farnesyl diphosphate (at pH 7.0)
{ECO:0000269|PubMed:10486140};
KM=1.3 uM for farnesyl diphosphate (at pH 9.0)
{ECO:0000269|PubMed:10486140};
KM=80 uM for magnesium (at pH 7.0)
{ECO:0000269|PubMed:10486140};
KM=80 uM for magnesium (at pH 9.0)
{ECO:0000269|PubMed:10486140};
pH dependence:
Optimum pH is 8.5-9.0. {ECO:0000269|PubMed:10486140};
-!- PATHWAY: Secondary metabolite biosynthesis; terpenoid
biosynthesis.
-!- TISSUE SPECIFICITY: Constitutively expressed in leaves and
flowers. {ECO:0000269|PubMed:10996256}.
-!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important
for the catalytic activity, presumably through binding to Mg(2+).
-!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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EMBL; AF157059; AAF80333.1; -; mRNA.
EMBL; AJ001539; CAC08805.1; -; mRNA.
EMBL; AJ249561; CAB56499.1; -; mRNA.
ProteinModelPortal; Q9LLR9; -.
SMR; Q9LLR9; -.
KEGG; ag:AAF80333; -.
KO; K14176; -.
BioCyc; MetaCyc:MONOMER-16025; -.
BRENDA; 4.2.3.39; 7150.
UniPathway; UPA00213; -.
GO; GO:0052682; F:epi-cedrol synthase activity; IEA:UniProtKB-EC.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
Gene3D; 1.10.600.10; -; 1.
Gene3D; 1.50.10.130; -; 1.
InterPro; IPR008949; Isoprenoid_synthase_dom.
InterPro; IPR034741; Terpene_cyclase_like_1_C.
InterPro; IPR001906; Terpene_synth_N.
InterPro; IPR036965; Terpene_synth_N_sf.
InterPro; IPR005630; Terpene_synthase_metal-bd.
InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
Pfam; PF01397; Terpene_synth; 1.
Pfam; PF03936; Terpene_synth_C; 1.
SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
SUPFAM; SSF48239; SSF48239; 1.
SUPFAM; SSF48576; SSF48576; 1.
1: Evidence at protein level;
Lyase; Magnesium; Manganese; Metal-binding.
CHAIN 1 547 Epi-cedrol synthase.
/FTId=PRO_0000380670.
MOTIF 299 303 DDXXD motif.
METAL 299 299 Magnesium or manganese 1. {ECO:0000250}.
METAL 299 299 Magnesium or manganese 2. {ECO:0000250}.
METAL 303 303 Magnesium or manganese 1. {ECO:0000250}.
METAL 303 303 Magnesium or manganese 2. {ECO:0000250}.
METAL 443 443 Magnesium or manganese 3. {ECO:0000250}.
METAL 447 447 Magnesium or manganese 3. {ECO:0000250}.
METAL 451 451 Magnesium or manganese 3. {ECO:0000250}.
CONFLICT 185 185 V -> I (in Ref. 3; CAB56499).
{ECO:0000305}.
SEQUENCE 547 AA; 63564 MW; E84EE9FCEED70BE2 CRC64;
MSLIVEDVIR PNANFPSEIW GDQFLAYDQD EQEGVEQVIK DLKEEVKSEL LTALNSPTQH
TELLKFIDAI ERLGIAYYFE EEINQVFQHM YTAYGDKWTG GNTSLWFRLM RQHGFFVSSD
IFSTYKDKEG RFKESLEKDV HGLLELYEAA YMFVPGEGIL DDALVFTRTC LDEIAKNPSL
SNSAVSSQIR EALTQPLHKR LPRLEALRYI PFYQQQASHS ETLLKLAKLG FNQLQSLHKK
ELSIISKWWK SFDVANNLPY ARNRPVECYF WALAVYFEPQ YSESRVFLSR FFSIQTFLDD
TYDAYGTYEE LEQFTEAIQR WSITCLDGLP ESMKLIFQML VKIFEEIEEI LSKDGKQHHV
NYIKETLKEA VQSYMTEARW AKEEYIPTIE EHTKVSYISI GYKLALVAGF ACMGDVIADD
SFEWVFTNPP LVNACCLLCR TMDDLGSHKG EQDRKHVAST IECYMKQFDA SEQQAYESLN
KKVEDAWKEI NREFMITCKD VNIHVAMRVL NFSRSVDVLY KNKDHFTHVG VEVINHIKSL
FVDAIIT


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