AMS1_ARTAN
ID AMS1_ARTAN Reviewed; 546 AA.
AC Q9AR04; A0A0G2R032; A0A0P0CC59; A0A1L7NYF5; A0A2U1M5G4; A2TEY7; C0KJU8;
AC C5HG79; Q306S5; Q9FVM5; Q9FY41; Q9LW98;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Amorpha-4,11-diene synthase {ECO:0000303|PubMed:11032404, ECO:0000303|PubMed:27273626};
DE EC=4.2.3.24 {ECO:0000269|PubMed:11032404, ECO:0000269|PubMed:11185551, ECO:0000269|PubMed:11289612};
GN Name=AMS1 {ECO:0000303|Ref.2};
GN Synonyms=ADS {ECO:0000303|PubMed:11032404, ECO:0000303|PubMed:27273626},
GN KCS12 {ECO:0000303|PubMed:11185551};
GN ORFNames=CTI12_AA415620 {ECO:0000312|EMBL:PWA56512.1};
OS Artemisia annua (Sweet wormwood).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC Artemisiinae; Artemisia.
OX NCBI_TaxID=35608;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC TISSUE=Leaf;
RX PubMed=11032404; DOI=10.1006/abbi.2000.1962;
RA Mercke P.E., Bengtsson M., Bouwmeester H.J., Posthumus M.A.,
RA Brodelius P.E.;
RT "Molecular cloning, expression, and characterization of a amorpha-4,11-
RT diene synthase from, a key enzyme of artemisinin biosynthesis of Artemisia
RT annua L.";
RL Arch. Biochem. Biophys. 381:173-180(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Leaf;
RA Liu Y., Ye H.C., Li G.F.;
RT "Cloning of sesquiterpene cyclase gene from Artemisia annua.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=11185551; DOI=10.1006/abbi.2000.2061;
RA Chang Y.-J., Song S.-H., Park S.-H., Kim S.-U.;
RT "Amorpha-4,11-diene synthase of Artemisia annua: cDNA isolation and
RT bacterial expression of a terpene synthase involved in artemisinin
RT biosynthesis.";
RL Arch. Biochem. Biophys. 383:178-184(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION BY REACTIVE OXYGEN SPECIES,
RP CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=11289612; DOI=10.1007/s004250000428;
RA Wallaart T.E., Bouwmeester H.J., Hille J., Poppinga L., Maijers N.C.A.;
RT "Amorpha-4,11-diene synthase: cloning and functional expression of a key
RT enzyme in the biosynthetic pathway of the novel antimalarial drug
RT artemisinin.";
RL Planta 212:460-465(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RA Huang Y., Feng L.L., Zeng Q.P.;
RT "Cloning and sequencing of amorpha-4,11-diene synthase cDNA of Artemisia
RT annua L.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kong J., Wang W., Cheng K.;
RT "Production of artemisinic acid by engineered yeast.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=20975893; DOI=10.6026/97320630004421;
RA Alam P., Kiran U., Ahmad M.M., Kamaluddin X., Khan M.A., Jhanwar S.,
RA Abdin M.Z.;
RT "Isolation, characterization and structural studies of amorpha-4,11-diene
RT synthase (ADS(3963)) from Artemisia annua L.";
RL Bioinformation 4:421-429(2010).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Banyai W., Supaibulwatana K.;
RT "Molecular cloning of amorpha4,11 diene synthase.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ahameethunisa A.R., Hopper W.;
RT "In planta expression of Artemisia annua sesquiterepene synthase, amorpha-
RT 4, 11-diene synthase in Cichorium intybus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sankhuan D., Chowpongpang S., Kirdmanee C., Supaibulwatana K.;
RT "Molecular cloning of amorpha 4,11 diene synthase.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Jhansi Rani S., Srinivasulu Y., Sujitha A., Usha R.;
RT "Molecular characterization of amorpha-4,11 diene synthase from Artemisia
RT annua L.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=27273626; DOI=10.1093/pcp/pcw094;
RA Muangphrom P., Seki H., Suzuki M., Komori A., Nishiwaki M., Mikawa R.,
RA Fukushima E.O., Muranaka T.;
RT "Functional analysis of amorpha-4,11-diene synthase (ADS) homologs from
RT non-artemisinin-producing Artemisia species: The discovery of novel
RT koidzumiol and (+)-alpha-bisabolol synthases.";
RL Plant Cell Physiol. 57:1678-1688(2016).
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Huhao1; TISSUE=Leaf;
RX PubMed=29703587; DOI=10.1016/j.molp.2018.03.015;
RA Shen Q., Zhang L., Liao Z., Wang S., Yan T., Shi P., Liu M., Fu X., Pan Q.,
RA Wang Y., Lv Z., Lu X., Zhang F., Jiang W., Ma Y., Chen M., Hao X., Li L.,
RA Tang Y., Lv G., Zhou Y., Sun X., Brodelius P.E., Rose J.K.C., Tang K.;
RT "The genome of Artemisia annua provides insight into the evolution of
RT Asteraceae family and artemisinin biosynthesis.";
RL Mol. Plant 11:776-788(2018).
RN [14]
RP NUCLEOTIDE SEQUENCE OF 1-35.
RA Yang R.Y., Feng L.L., Yang X.Q., Zeng Q.P.;
RT "ADS promoter-driven GUS phenotyping in Nicotiana tabacum: a surveillance
RT system on stress-induced expression of artemisinin biosynthesis responsible
RT genes.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10626375; DOI=10.1016/s0031-9422(99)00206-x;
RA Bouwmeester H.J., Wallaart T.E., Janssen M.H., van Loo B., Jansen B.J.,
RA Posthumus M.A., Schmidt C.O., De Kraker J.W., Koenig W.A., Franssen M.C.;
RT "Amorpha-4,11-diene synthase catalyses the first probable step in
RT artemisinin biosynthesis.";
RL Phytochemistry 52:843-854(1999).
RN [16]
RP BIOTECHNOLOGY.
RX PubMed=16612385; DOI=10.1038/nature04640;
RA Ro D.-K., Paradise E.M., Ouellet M., Fisher K.J., Newman K.L., Ndungu J.M.,
RA Ho K.A., Eachus R.A., Ham T.S., Kirby J., Chang M.C.Y., Withers S.T.,
RA Shiba Y., Sarpong R., Keasling J.D.;
RT "Production of the antimalarial drug precursor artemisinic acid in
RT engineered yeast.";
RL Nature 440:940-943(2006).
RN [17]
RP TISSUE SPECIFICITY.
RX PubMed=19664791; DOI=10.1016/j.phytochem.2009.07.009;
RA Olsson M.E., Olofsson L.M., Lindahl A.-L., Lundgren A., Brodelius M.,
RA Brodelius P.E.;
RT "Localization of enzymes of artemisinin biosynthesis to the apical cells of
RT glandular secretory trichomes of Artemisia annua L.";
RL Phytochemistry 70:1123-1128(2009).
RN [18]
RP INDUCTION BY GIBBERELLIC ACID.
RX DOI=10.1007/s10725-010-9510-9;
RA Banyai W., Mii M., Supaibulwatana K.;
RT "Enhancement of artemisinin content and biomass in Artemisia annua by
RT exogenous GA3 treatment.";
RL Plant Growth Regul. 63:45-54(2011).
RN [19]
RP TISSUE SPECIFICITY.
RX PubMed=22195571; DOI=10.1016/j.plantsci.2011.10.019;
RA Olofsson L., Lundgren A., Brodelius P.E.;
RT "Trichome isolation with and without fixation using laser microdissection
RT and pressure catapulting followed by RNA amplification: expression of genes
RT of terpene metabolism in apical and sub-apical trichome cells of Artemisia
RT annua L.";
RL Plant Sci. 183:9-13(2012).
RN [20]
RP BIOTECHNOLOGY.
RX PubMed=22247290; DOI=10.1073/pnas.1110740109;
RA Westfall P.J., Pitera D.J., Lenihan J.R., Eng D., Woolard F.X.,
RA Regentin R., Horning T., Tsuruta H., Melis D.J., Owens A., Fickes S.,
RA Diola D., Benjamin K.R., Keasling J.D., Leavell M.D., McPhee D.J.,
RA Renninger N.S., Newman J.D., Paddon C.J.;
RT "Production of amorphadiene in yeast, and its conversion to
RT dihydroartemisinic acid, precursor to the antimalarial agent artemisinin.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E111-E118(2012).
RN [21]
RP BIOTECHNOLOGY.
RX PubMed=23575629; DOI=10.1038/nature12051;
RA Paddon C.J., Westfall P.J., Pitera D.J., Benjamin K., Fisher K., McPhee D.,
RA Leavell M.D., Tai A., Main A., Eng D., Polichuk D.R., Teoh K.H., Reed D.W.,
RA Treynor T., Lenihan J., Fleck M., Bajad S., Dang G., Diola D., Dorin G.,
RA Ellens K.W., Fickes S., Galazzo J., Gaucher S.P., Geistlinger T., Henry R.,
RA Hepp M., Horning T., Iqbal T., Jiang H., Kizer L., Lieu B., Melis D.,
RA Moss N., Regentin R., Secrest S., Tsuruta H., Vazquez R., Westblade L.F.,
RA Xu L., Yu M., Zhang Y., Zhao L., Lievense J., Covello P.S., Keasling J.D.,
RA Reiling K.K., Renninger N.S., Newman J.D.;
RT "High-level semi-synthetic production of the potent antimalarial
RT artemisinin.";
RL Nature 496:528-532(2013).
RN [22]
RP REVIEW ON ARTEMISININ ANTIMALARIAL PROPERTIES.
RX PubMed=27488942; DOI=10.1002/anie.201601967;
RA Tu Y.;
RT "Artemisinin-A Gift from Traditional Chinese Medicine to the World (Nobel
RT Lecture).";
RL Angew. Chem. Int. Ed. 55:10210-10226(2016).
RN [23]
RP TISSUE SPECIFICITY.
RX PubMed=30851440; DOI=10.1016/j.molp.2019.02.011;
RA Judd R., Bagley M.C., Li M., Zhu Y., Lei C., Yuzuak S., Ekeloef M., Pu G.,
RA Zhao X., Muddiman D.C., Xie D.-Y.;
RT "Artemisinin biosynthesis in non-glandular trichome cells of Artemisia
RT annua.";
RL Mol. Plant 12:704-714(2019).
RN [24]
RP PATHWAY, AND REVIEW.
RX PubMed=30468448; DOI=10.1039/c8np00077h;
RA Liu Y., Jing S.-X., Luo S.-H., Li S.-H.;
RT "Non-volatile natural products in plant glandular trichomes: chemistry,
RT biological activities and biosynthesis.";
RL Nat. Prod. Rep. 36:626-665(2019).
RN [25]
RP BIOTECHNOLOGY.
RX PubMed=32514287; DOI=10.1186/s13020-020-00336-8;
RA Uzun T., Toptas O.;
RT "Artesunate: could be an alternative drug to chloroquine in COVID-19
RT treatment?";
RL Chin. Med. J. 15:54-54(2020).
RN [26]
RP BIOTECHNOLOGY, AND REVIEW.
RX PubMed=32405226; DOI=10.1016/j.phrs.2020.104901;
RA Cheong D.H.J., Tan D.W.S., Wong F.W.S., Tran T.;
RT "Anti-malarial drug, artemisinin and its derivatives for the treatment of
RT respiratory diseases.";
RL Pharmacol. Res. 158:104901-104901(2020).
CC -!- FUNCTION: Involved in the biosynthesis of the antimalarial endoperoxide
CC artemisinin (PubMed:11032404, PubMed:11185551, PubMed:11289612,
CC PubMed:10626375, PubMed:27488942). Catalyzes the formation of both
CC olefinic and oxygenated sesquiterpenes, with amorpha-4,11-diene being
CC the major product (PubMed:11032404, PubMed:11185551, PubMed:11289612,
CC PubMed:10626375). {ECO:0000269|PubMed:10626375,
CC ECO:0000269|PubMed:11032404, ECO:0000269|PubMed:11185551,
CC ECO:0000269|PubMed:11289612, ECO:0000303|PubMed:27488942}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (+)-amorpha-4,11-diene +
CC diphosphate; Xref=Rhea:RHEA:18325, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:52026, ChEBI:CHEBI:175763; EC=4.2.3.24;
CC Evidence={ECO:0000269|PubMed:11032404, ECO:0000269|PubMed:11185551,
CC ECO:0000269|PubMed:11289612};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18326;
CC Evidence={ECO:0000269|PubMed:11032404, ECO:0000269|PubMed:11185551,
CC ECO:0000269|PubMed:11289612};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:A0A1C9J6A7};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.6 uM for farnesyl diphosphate (at 30 degrees Celsius)
CC {ECO:0000269|PubMed:10626375};
CC KM=9 uM for farnesyl diphosphate (at pH 7.5)
CC {ECO:0000269|PubMed:11032404};
CC KM=70 uM for magnesium ions {ECO:0000269|PubMed:11032404};
CC KM=13 uM for manganese ions {ECO:0000269|PubMed:11032404};
CC pH dependence:
CC Optimum pH is 7.5-9 (PubMed:11032404). Optimum pH is 6.5-7 (at 30
CC degrees Celsius) (PubMed:10626375). {ECO:0000269|PubMed:10626375,
CC ECO:0000269|PubMed:11032404};
CC -!- PATHWAY: Sesquiterpene biosynthesis. {ECO:0000303|PubMed:30468448}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed both in apical and sub-apical cells of
CC glandular secretory trichomes. Also present in non-glandular trichome
CC cells (PubMed:30851440). {ECO:0000269|PubMed:19664791,
CC ECO:0000269|PubMed:22195571, ECO:0000269|PubMed:30851440}.
CC -!- INDUCTION: By exposure to reactive oxygen species (PubMed:11289612).
CC Strongly induced by gibberellic acid (GA(3)) leading to an increased
CC artemisinin yield (Ref.18). {ECO:0000269|PubMed:11289612,
CC ECO:0000269|Ref.18}.
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|UniProtKB:A0A1C9J6A7}.
CC -!- BIOTECHNOLOGY: Artemisinin and derivatives (e.g. artesunate), are
CC antimalarial drugs due to their endoperoxidase properties; they also
CC display multiple pharmacological actions against inflammation,viral
CC infections, and cell and tumor proliferation (PubMed:32514287,
CC PubMed:32405226). Artesunate may be a promising treatment for COVID-19
CC mediated by the severe acute respiratory syndrome coronavirus 2 (2019-
CC nCoV) (SARS-CoV-2) because of its anti-inflammatory activity, NF-kappaB
CC (nuclear factor kappa B)-coronavirus effect and chloroquine-like
CC endocytosis inhibition mechanism (PubMed:32514287, PubMed:32405226).
CC {ECO:0000303|PubMed:32405226, ECO:0000303|PubMed:32514287}.
CC -!- BIOTECHNOLOGY: Yeast (S.cerevisiae) has been engineered to produce
CC artemisinic-acid, a precursor of the antimalarial artemisinin compound,
CC by expressing AMS1/ADS, CYP71AV1, ADH1 and ALDH1 in conjunction with
CC CYB5 and CPR1. {ECO:0000269|PubMed:16612385,
CC ECO:0000269|PubMed:22247290, ECO:0000269|PubMed:23575629}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACL15394.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ALJ03212.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=PWA56512.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF138959; AAF61439.1; -; mRNA.
DR EMBL; AF327527; AAK15697.1; -; Genomic_DNA.
DR EMBL; AF327526; AAK15696.1; -; mRNA.
DR EMBL; AJ251751; CAB94691.1; -; mRNA.
DR EMBL; AY006482; AAF98444.1; -; mRNA.
DR EMBL; DQ241826; ABB51572.1; -; mRNA.
DR EMBL; EF197888; ABM88787.1; -; mRNA.
DR EMBL; FJ432667; ACL15394.1; ALT_SEQ; Genomic_DNA.
DR EMBL; HQ315833; ADU25497.1; -; mRNA.
DR EMBL; JQ319661; AFA34434.1; -; mRNA.
DR EMBL; KJ609176; AIC83777.1; -; mRNA.
DR EMBL; KR445687; ALJ03212.1; ALT_INIT; mRNA.
DR EMBL; LC106014; BAW34953.1; -; Genomic_DNA.
DR EMBL; PKPP01006435; PWA56512.1; ALT_SEQ; Genomic_DNA.
DR EMBL; FJ613423; ACM80358.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9AR04; -.
DR SMR; Q9AR04; -.
DR PRIDE; Q9AR04; -.
DR KEGG; ag:AAF98444; -.
DR BioCyc; MetaCyc:MON-12183; -.
DR BRENDA; 4.2.3.24; 7150.
DR Proteomes; UP000245207; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0034006; F:amorpha-4,11-diene 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:0009739; P:response to gibberellin; IEP:UniProtKB.
DR GO; GO:0000302; P:response to reactive oxygen species; IEP:UniProtKB.
DR GO; GO:0051761; P:sesquiterpene 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 Cytoplasm; Lyase; Magnesium; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..546
FT /note="Amorpha-4,11-diene synthase"
FT /id="PRO_0000248160"
FT MOTIF 299..303
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 440
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 443
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 447
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 451
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT CONFLICT 24
FT /note="F -> S (in Ref. 5; ABB51572)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="E -> D (in Ref. 13; PWA56512)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="E -> Q (in Ref. 4; AAF98444)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="N -> K (in Ref. 13; PWA56512)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="A -> V (in Ref. 10; AIC83777)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="L -> P (in Ref. 13; PWA56512)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="R -> Q (in Ref. 2; AAK15696/AAK15697, 7; ACL15394
FT and 13; PWA56512)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="W -> Y (in Ref. 13; PWA56512)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="N -> D (in Ref. 2; AAK15696/AAK15697 and 7;
FT ACL15394)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="R -> H (in Ref. 13; PWA56512)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="N -> D (in Ref. 2; AAK15696/AAK15697 and 7;
FT ACL15394)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="I -> T (in Ref. 5; ABB51572)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="I -> M (in Ref. 2; AAK15696/AAK15697 and 7;
FT ACL15394)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="I -> M (in Ref. 3; CAB94691)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="D -> Y (in Ref. 13; PWA56512)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="H -> Q (in Ref. 13; PWA56512)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="V -> A (in Ref. 10; AIC83777)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="Y -> F (in Ref. 2; AAK15696/AAK15697, 3; CAB94691,
FT 7; ACL15394 and 13; PWA56512)"
FT /evidence="ECO:0000305"
FT CONFLICT 289..291
FT /note="TKA -> AKV (in Ref. 13; PWA56512)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="L -> F (in Ref. 13; PWA56512)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="F -> T (in Ref. 13; PWA56512)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="R -> K (in Ref. 13; PWA56512)"
FT /evidence="ECO:0000305"
FT CONFLICT 367..373
FT /note="VKEFVRN -> MKEFIRG (in Ref. 13; PWA56512)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="V -> F (in Ref. 6; ABM88787, 8; ADU25497, 9;
FT AFA34434 and 11; ALJ03212)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="K -> N (in Ref. 5; ABB51572)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="E -> V (in Ref. 13; PWA56512)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="G -> D (in Ref. 5; ABB51572)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="S -> F (in Ref. 13; PWA56512)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="N -> D (in Ref. 5; ABB51572)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="V -> F (in Ref. 13; PWA56512)"
FT /evidence="ECO:0000305"
FT CONFLICT 507
FT /note="A -> V (in Ref. 13; PWA56512)"
FT /evidence="ECO:0000305"
FT CONFLICT 545
FT /note="S -> G (in Ref. 10; AIC83777)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 546 AA; 63933 MW; 381386A7ED81FEF9 CRC64;
MSLTEEKPIR PIANFPPSIW GDQFLIYEKQ VEQGVEQIVN DLKKEVRQLL KEALDIPMKH
ANLLKLIDEI QRLGIPYHFE REIDHALQCI YETYGDNWNG DRSSLWFRLM RKQGYYVTCD
VFNNYKDKNG AFKQSLANDV EGLLELYEAT SMRVPGEIIL EDALGFTRSR LSIMTKDAFS
TNPALFTEIQ RALKQPLWKR LPRIEAAQYI PFYQQQDSHN KTLLKLAKLE FNLLQSLHKE
ELSHVCKWWK AFDIKKNAPC LRDRIVECYF WGLGSGYEPQ YSRARVFFTK AVAVITLIDD
TYDAYGTYEE LKIFTEAVER WSITCLDTLP EYMKPIYKLF MDTYTEMEEF LAKEGRTDLF
NCGKEFVKEF VRNLMVEAKW ANEGHIPTTE EHDPVVIITG GANLLTTTCY LGMSDIFTKE
SVEWAVSAPP LFRYSGILGR RLNDLMTHKA EQERKHSSSS LESYMKEYNV NEEYAQTLIY
KEVEDVWKDI NREYLTTKNI PRPLLMAVIY LCQFLEVQYA GKDNFTRMGD EYKHLIKSLL
VYPMSI
