TPSDV_ABIGR
ID TPSDV_ABIGR Reviewed; 868 AA.
AC Q38710; Q94FW1;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Bifunctional abietadiene synthase, chloroplastic;
DE AltName: Full=(-)-abieta-7(8),13(14)-diene synthase;
DE AltName: Full=Abietadiene cyclase;
DE Short=AgAS;
DE AltName: Full=Agggabi;
DE Includes:
DE RecName: Full=Abietadiene synthase;
DE EC=4.2.3.18 {ECO:0000269|PubMed:10814381, ECO:0000269|PubMed:11112547};
DE AltName: Full=Neoabietadiene synthase;
DE EC=4.2.3.132 {ECO:0000269|PubMed:10814381, ECO:0000269|PubMed:11112547};
DE Includes:
DE RecName: Full=Copalyl diphosphate synthase;
DE EC=5.5.1.12 {ECO:0000269|PubMed:10814381, ECO:0000269|PubMed:11112547};
DE Flags: Precursor;
GN Name=AS; Synonyms=ac22, ag22;
OS Abies grandis (Grand fir) (Pinus grandis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Abies.
OX NCBI_TaxID=46611;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 148-166; 522-530; 615-625
RP AND 699-705, AND INDUCTION.
RC TISSUE=Stem;
RX PubMed=8798524; DOI=10.1074/jbc.271.38.23262;
RA Stoffer Vogel B., Wildung M.R., Vogel G., Croteau R.B.;
RT "Abietadiene synthase from grand fir (Abies grandis). cDNA isolation,
RT characterization, and bacterial expression of a bifunctional diterpene
RT cyclase involved in resin acid biosynthesis.";
RL J. Biol. Chem. 271:23262-23268(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-868, AND NOMENCLATURE.
RX PubMed=11404343; DOI=10.1093/genetics/158.2.811;
RA Trapp S.C., Croteau R.B.;
RT "Genomic organization of plant terpene synthases and molecular evolutionary
RT implications.";
RL Genetics 158:811-832(2001).
RN [3]
RP GENE FAMILY, NOMENCLATURE, AND FUNCTION.
RX PubMed=9539701; DOI=10.1073/pnas.95.8.4126;
RA Bohlmann J., Meyer-Gauen G., Croteau R.B.;
RT "Plant terpenoid synthases: molecular biology and phylogenetic analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:4126-4133(1998).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RX PubMed=11112547; DOI=10.1021/bi001997l;
RA Peters R.J., Flory J.E., Jetter R., Ravn M.M., Lee H.J., Coates R.M.,
RA Croteau R.B.;
RT "Abietadiene synthase from grand fir (Abies grandis): characterization and
RT mechanism of action of the 'pseudomature' recombinant enzyme.";
RL Biochemistry 39:15592-15602(2000).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10814381; DOI=10.1021/ol991230p;
RA Ravn M.M., Coates R.M., Flory J.E., Peters R.J., Croteau R.;
RT "Stereochemistry of the cyclization-rearrangement of (+)-copalyl
RT diphosphate to (-)-abietadiene catalyzed by recombinant abietadiene
RT synthase from Abies grandis.";
RL Org. Lett. 2:573-576(2000).
RN [6]
RP MUTAGENESIS OF ASP-404 AND ASP-621, AND CHARACTERIZATION.
RX PubMed=11552804; DOI=10.1021/ja010670k;
RA Peters R.J., Ravn M.M., Coates R.M., Croteau R.B.;
RT "Bifunctional abietadiene synthase: free diffusive transfer of the (+)-
RT copalyl diphosphate intermediate between two distinct active sites.";
RL J. Am. Chem. Soc. 123:8974-8978(2001).
RN [7]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, 3D-STRUCTURE MODELING, AND
RP MUTAGENESIS OF TRP-358; ASP-361; ARG-365; ASP-402; ASP-404; ASP-405;
RP ARG-411; ARG-454; GLU-499 AND TYR-520.
RX PubMed=11827528; DOI=10.1021/bi011879d;
RA Peters R.J., Croteau R.B.;
RT "Abietadiene synthase catalysis: conserved residues involved in
RT protonation-initiated cyclization of geranylgeranyl diphosphate to (+)-
RT copalyl diphosphate.";
RL Biochemistry 41:1836-1842(2002).
RN [8]
RP MUTAGENESIS OF ARG-584; ARG-586; GLU-589; THR-617; ASP-621; ASP-625;
RP GLU-699; SER-721; ARG-762; ASN-765; ASP-766; THR-769; GLU-773; GLU-778;
RP TYR-841; ASP-845 AND THR-848, AND CHARACTERIZATION.
RX PubMed=11805316; DOI=10.1073/pnas.022627099;
RA Peters R.J., Croteau R.B.;
RT "Abietadiene synthase catalysis: mutational analysis of a prenyl
RT diphosphate ionization-initiated cyclization and rearrangement.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:580-584(2002).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF LYS-86 AND ARG-87.
RX PubMed=12614165; DOI=10.1021/bi020492n;
RA Peters R.J., Carter O.A., Zhang Y., Matthews B.W., Croteau R.B.;
RT "Bifunctional abietadiene synthase: mutual structural dependence of the
RT active sites for protonation-initiated and ionization-initiated
RT cyclizations.";
RL Biochemistry 42:2700-2707(2003).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF ALA-723.
RX PubMed=18052062; DOI=10.1021/ja074977g;
RA Wilderman P.R., Peters R.J.;
RT "A single residue switch converts abietadiene synthase into a pimaradiene
RT specific cyclase.";
RL J. Am. Chem. Soc. 129:15736-15737(2007).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF ARG-356 AND ASP-621.
RX PubMed=20430888; DOI=10.1074/jbc.m110.123307;
RA Mann F.M., Prisic S., Davenport E.K., Determan M.K., Coates R.M.,
RA Peters R.J.;
RT "A single residue switch for Mg(2+)-dependent inhibition characterizes
RT plant class II diterpene cyclases from primary and secondary metabolism.";
RL J. Biol. Chem. 285:20558-20563(2010).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 85-868, AND MUTAGENESIS OF
RP ASN-451 AND VAL-727.
RX PubMed=22219188; DOI=10.1074/jbc.m111.337592;
RA Zhou K., Gao Y., Hoy J.A., Mann F.M., Honzatko R.B., Peters R.J.;
RT "Insights into diterpene cyclization from structure of bifunctional
RT abietadiene synthase from Abies grandis.";
RL J. Biol. Chem. 287:6840-6850(2012).
CC -!- FUNCTION: Involved in defensive oleoresin formation in conifers in
CC response to insect attack or other injury. Involved in diterpene (C20)
CC olefins biosynthesis. Bifunctional enzyme that catalyzes two sequential
CC cyclizations of geranylgeranyl diphosphate (GGPP) to abietadiene. The
CC copalyl diphosphate (CPP) intermediate diffuses freely between the 2
CC active sites in the enzyme. Changes in reaction pH, but not salt
CC concentration, influence the relative proportion of the major products
CC of the enzyme, abitadiene, levopimaradiene and neoabitadiene.
CC {ECO:0000269|PubMed:10814381, ECO:0000269|PubMed:11112547,
CC ECO:0000269|PubMed:11827528, ECO:0000269|PubMed:12614165,
CC ECO:0000269|PubMed:18052062, ECO:0000269|PubMed:20430888,
CC ECO:0000269|PubMed:9539701}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = (+)-copalyl
CC diphosphate; Xref=Rhea:RHEA:24316, ChEBI:CHEBI:58635,
CC ChEBI:CHEBI:58756; EC=5.5.1.12;
CC Evidence={ECO:0000269|PubMed:10814381, ECO:0000269|PubMed:11112547};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(+)-copalyl diphosphate = abieta-7,13-diene + diphosphate;
CC Xref=Rhea:RHEA:13873, ChEBI:CHEBI:30232, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58635; EC=4.2.3.18;
CC Evidence={ECO:0000269|PubMed:10814381, ECO:0000269|PubMed:11112547};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(+)-copalyl diphosphate = diphosphate + neoabietadiene;
CC Xref=Rhea:RHEA:33987, ChEBI:CHEBI:29651, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58635; EC=4.2.3.132;
CC Evidence={ECO:0000269|PubMed:10814381, ECO:0000269|PubMed:11112547};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q40577};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q40577};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC -!- ACTIVITY REGULATION: Not inhibited by 13-cyclopropylidene or 16-
CC methylidenegeranylgeranyl diphosphate. The copalyl diphosphate synthase
CC activity is not susceptible to magnesium-dependent inhibition.
CC {ECO:0000269|PubMed:11112547}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3 uM for GGPP (in presence of magnesium)
CC {ECO:0000269|PubMed:11112547, ECO:0000269|PubMed:11827528};
CC KM=20 uM for GGPP (in absence of magnesium)
CC {ECO:0000269|PubMed:11112547, ECO:0000269|PubMed:11827528};
CC KM=0.4 uM for CPP (in presence of magnesium)
CC {ECO:0000269|PubMed:11112547, ECO:0000269|PubMed:11827528};
CC KM=10 uM for CPP (in absence of magnesium)
CC {ECO:0000269|PubMed:11112547, ECO:0000269|PubMed:11827528};
CC pH dependence:
CC Optimum pH is 7.2 with GGPP as substrate and 8.7 with CPP as
CC substrate. {ECO:0000269|PubMed:11112547,
CC ECO:0000269|PubMed:11827528};
CC -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC -!- INDUCTION: By wounding. {ECO:0000269|PubMed:8798524}.
CC -!- DOMAIN: The Asp-Xaa-Asp-Asp (DXDD) motif is important for the catalytic
CC activity in the class II active site relevant for the cyclization of
CC GGPP. The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the
CC catalytic activity in the class I active site, presumably through
CC binding to Mg(2+). {ECO:0000305}.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: The abietadiene synthase activity exhibits an absolute
CC dependence on a divalent metal ion cofactor while the copalyl
CC diphosphate synthase activity is not completely dependent.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily.
CC {ECO:0000305}.
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DR EMBL; U50768; AAB05407.1; -; mRNA.
DR EMBL; AF326516; AAK83563.1; -; Genomic_DNA.
DR PDB; 3S9V; X-ray; 2.30 A; A/B/C/D=85-868.
DR PDBsum; 3S9V; -.
DR AlphaFoldDB; Q38710; -.
DR SMR; Q38710; -.
DR KEGG; ag:AAB05407; -.
DR BioCyc; MetaCyc:MON-12822; -.
DR BRENDA; 4.2.3.132; 2.
DR BRENDA; 4.2.3.18; 2.
DR UniPathway; UPA00924; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0050554; F:abietadiene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0050559; F:copalyl diphosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; 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; 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 SUPFAM; SSF48239; SSF48239; 2.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Direct protein sequencing; Isomerase; Lyase;
KW Magnesium; Manganese; Metal-binding; Multifunctional enzyme; Plastid;
KW Transit peptide.
FT TRANSIT 1..70
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 71..868
FT /note="Bifunctional abietadiene synthase, chloroplastic"
FT /id="PRO_0000033634"
FT MOTIF 402..405
FT /note="DXDD motif"
FT /evidence="ECO:0000305"
FT MOTIF 621..625
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 402
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 404
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 489
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 621
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 621
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 625
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 625
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 765
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 769
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 773
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT MUTAGEN 86
FT /note="K->A: No effect on CPP binding, but decreased
FT abietadiene synthase activity; when associated with A-87."
FT /evidence="ECO:0000269|PubMed:12614165"
FT MUTAGEN 87
FT /note="R->A: No effect on CPP binding, but decreased
FT abietadiene synthase activity; when associated with A-86."
FT /evidence="ECO:0000269|PubMed:12614165"
FT MUTAGEN 356
FT /note="R->A: No effect on abietadiene synthase activity,
FT but strongly reduced copalyl diphosphate synthase
FT activity."
FT /evidence="ECO:0000269|PubMed:20430888"
FT MUTAGEN 356
FT /note="R->H: Increased Mg(2+) inhibition; when associated
FT with A-621."
FT /evidence="ECO:0000269|PubMed:20430888"
FT MUTAGEN 358
FT /note="W->A: Decreased copalyl diphosphate synthase
FT activity."
FT /evidence="ECO:0000269|PubMed:11827528"
FT MUTAGEN 361
FT /note="D->A: No effect on GGPP binding, but decreased
FT copalyl diphosphate synthase activity."
FT /evidence="ECO:0000269|PubMed:11827528"
FT MUTAGEN 365
FT /note="R->A: No effect on GGPP binding, but decreased
FT copalyl diphosphate synthase activity."
FT /evidence="ECO:0000269|PubMed:11827528"
FT MUTAGEN 402
FT /note="D->A,E,N: No effect on GGPP binding, but decreased
FT copalyl diphosphate synthase activity."
FT /evidence="ECO:0000269|PubMed:11827528"
FT MUTAGEN 404
FT /note="D->A,E,N: No effect on GGPP binding, but loss of
FT copalyl diphosphate synthase activity."
FT /evidence="ECO:0000269|PubMed:11552804,
FT ECO:0000269|PubMed:11827528"
FT MUTAGEN 405
FT /note="D->A,E,N: No effect on GGPP binding, but decreased
FT copalyl diphosphate synthase activity."
FT /evidence="ECO:0000269|PubMed:11827528"
FT MUTAGEN 411
FT /note="R->A: No effect on GGPP binding, but slightly
FT decreased copalyl diphosphate synthase activity."
FT /evidence="ECO:0000269|PubMed:11827528"
FT MUTAGEN 451
FT /note="N->A: No effect on abietadiene synthase activity,
FT but strongly reduced copalyl diphosphate synthase
FT activity."
FT /evidence="ECO:0000269|PubMed:22219188"
FT MUTAGEN 454
FT /note="R->A: No effect on GGPP binding, but decreased
FT copalyl diphosphate synthase activity."
FT /evidence="ECO:0000269|PubMed:11827528"
FT MUTAGEN 499
FT /note="E->A: No effect on GGPP binding, but decreased
FT copalyl diphosphate synthase activity."
FT /evidence="ECO:0000269|PubMed:11827528"
FT MUTAGEN 520
FT /note="Y->A: No effect on GGPP binding, but slightly
FT decreased copalyl diphosphate synthase activity."
FT /evidence="ECO:0000269|PubMed:11827528"
FT MUTAGEN 584
FT /note="R->A: No or small effect on substrate binding, but
FT strongly decreases abietadiene synthase activity."
FT /evidence="ECO:0000269|PubMed:11805316"
FT MUTAGEN 586
FT /note="R->A: No or small effect on substrate binding, but
FT strongly decreases abietadiene synthase activity."
FT /evidence="ECO:0000269|PubMed:11805316"
FT MUTAGEN 589
FT /note="E->A: Lower substrate binding and strong decrease of
FT abietadiene synthase activity."
FT /evidence="ECO:0000269|PubMed:11805316"
FT MUTAGEN 617
FT /note="T->A: Increased production of abietadiene at the
FT expense of levopimaradiene."
FT /evidence="ECO:0000269|PubMed:11805316"
FT MUTAGEN 621
FT /note="D->A: Loss of abietadiene synthase activity.
FT Increased Mg(2+) inhibition; when associated with H-356."
FT /evidence="ECO:0000269|PubMed:11552804,
FT ECO:0000269|PubMed:11805316, ECO:0000269|PubMed:20430888"
FT MUTAGEN 625
FT /note="D->A: No or small effect on substrate binding, but
FT strongly decreases abietadiene synthase activity."
FT /evidence="ECO:0000269|PubMed:11805316"
FT MUTAGEN 699
FT /note="E->A: No or small effect on substrate binding, but
FT strongly decreases abietadiene synthase activity."
FT /evidence="ECO:0000269|PubMed:11805316"
FT MUTAGEN 721
FT /note="S->A: Lower substrate binding and strong decrease of
FT abietadiene synthase activity."
FT /evidence="ECO:0000269|PubMed:11805316"
FT MUTAGEN 723
FT /note="A->S: Produces pimaradienes instead of
FT abietadienes."
FT /evidence="ECO:0000269|PubMed:18052062"
FT MUTAGEN 727
FT /note="V->T: No effect."
FT /evidence="ECO:0000269|PubMed:22219188"
FT MUTAGEN 762
FT /note="R->A: No or small effect on substrate binding, but
FT strongly decreases abietadiene synthase activity."
FT /evidence="ECO:0000269|PubMed:11805316"
FT MUTAGEN 765
FT /note="N->A: Abolishes the conversion of CPP to
FT abietadiene; produces only sandaracopimaradiene."
FT /evidence="ECO:0000269|PubMed:11805316"
FT MUTAGEN 766
FT /note="D->A: No or small effect on substrate binding, but
FT strongly decreases abietadiene synthase activity."
FT /evidence="ECO:0000269|PubMed:11805316"
FT MUTAGEN 769
FT /note="T->A: Increased production of neoabietadiene at the
FT expense of both levopimaradiene and abietadiene."
FT /evidence="ECO:0000269|PubMed:11805316"
FT MUTAGEN 773
FT /note="E->A: Increased production of neoabietadiene."
FT /evidence="ECO:0000269|PubMed:11805316"
FT MUTAGEN 778
FT /note="E->A: No or small effect on substrate binding, but
FT strongly decreases abietadiene synthase activity."
FT /evidence="ECO:0000269|PubMed:11805316"
FT MUTAGEN 841
FT /note="Y->F: No or small effect on substrate binding, but
FT strongly decreases abietadiene synthase activity."
FT /evidence="ECO:0000269|PubMed:11805316"
FT MUTAGEN 845
FT /note="D->A: No or small effect on substrate binding, but
FT strongly decreases abietadiene synthase activity."
FT /evidence="ECO:0000269|PubMed:11805316"
FT MUTAGEN 848
FT /note="T->A: No or small effect on substrate binding, but
FT strongly decreases abietadiene synthase activity."
FT /evidence="ECO:0000269|PubMed:11805316"
FT CONFLICT 23
FT /note="A -> T (in Ref. 2; AAK83563)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="F -> S (in Ref. 2; AAK83563)"
FT /evidence="ECO:0000305"
FT CONFLICT 297..299
FT /note="DWQ -> EWE (in Ref. 2; AAK83563)"
FT /evidence="ECO:0000305"
FT CONFLICT 557
FT /note="V -> L (in Ref. 2; AAK83563)"
FT /evidence="ECO:0000305"
FT CONFLICT 579
FT /note="D -> E (in Ref. 2; AAK83563)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="Q -> K (in Ref. 2; AAK83563)"
FT /evidence="ECO:0000305"
FT HELIX 112..129
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 139..145
FT /evidence="ECO:0007829|PDB:3S9V"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 160..168
FT /evidence="ECO:0007829|PDB:3S9V"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 184..200
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 205..219
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 220..224
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 234..247
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 257..270
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 275..280
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 284..291
FT /evidence="ECO:0007829|PDB:3S9V"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 298..302
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 315..325
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 328..341
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 352..365
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 369..372
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 373..384
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 403..415
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 422..428
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 446..456
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 464..480
FT /evidence="ECO:0007829|PDB:3S9V"
FT TURN 481..483
FT /evidence="ECO:0007829|PDB:3S9V"
FT STRAND 492..494
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 496..505
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 508..510
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 513..523
FT /evidence="ECO:0007829|PDB:3S9V"
FT STRAND 530..536
FT /evidence="ECO:0007829|PDB:3S9V"
FT TURN 539..541
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 544..574
FT /evidence="ECO:0007829|PDB:3S9V"
FT TURN 575..578
FT /evidence="ECO:0007829|PDB:3S9V"
FT STRAND 581..583
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 587..597
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 601..603
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 604..624
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 630..642
FT /evidence="ECO:0007829|PDB:3S9V"
FT STRAND 644..647
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 648..650
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 653..677
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 682..704
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 711..721
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 724..731
FT /evidence="ECO:0007829|PDB:3S9V"
FT STRAND 735..737
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 741..744
FT /evidence="ECO:0007829|PDB:3S9V"
FT TURN 745..747
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 752..776
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 782..789
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 795..819
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 824..840
FT /evidence="ECO:0007829|PDB:3S9V"
FT HELIX 851..863
FT /evidence="ECO:0007829|PDB:3S9V"
SQ SEQUENCE 868 AA; 99536 MW; AD5E79F56B70D25C CRC64;
MAMPSSSLSS QIPTAAHHLT ANAQSIPHFS TTLNAGSSAS KRRSLYLRWG KGSNKIIACV
GEGGATSVPY QSAEKNDSLS SSTLVKREFP PGFWKDDLID SLTSSHKVAA SDEKRIETLI
SEIKNMFRCM GYGETNPSAY DTAWVARIPA VDGSDNPHFP ETVEWILQNQ LKDGSWGEGF
YFLAYDRILA TLACIITLTL WRTGETQVQK GIEFFRTQAG KMEDEADSHR PSGFEIVFPA
MLKEAKILGL DLPYDLPFLK QIIEKREAKL KRIPTDVLYA LPTTLLYSLE GLQEIVDWQK
IMKLQSKDGS FLSSPASTAA VFMRTGNKKC LDFLNFVLKK FGNHVPCHYP LDLFERLWAV
DTVERLGIDR HFKEEIKEAL DYVYSHWDER GIGWARENPV PDIDDTAMGL RILRLHGYNV
SSDVLKTFRD ENGEFFCFLG QTQRGVTDML NVNRCSHVSF PGETIMEEAK LCTERYLRNA
LENVDAFDKW AFKKNIRGEV EYALKYPWHK SMPRLEARSY IENYGPDDVW LGKTVYMMPY
ISNEKYLELA KLDFNKVQSI HQTELQDLRR WWKSSGFTDL NFTRERVTEI YFSPASFIFE
PEFSKCREVY TKTSNFTVIL DDLYDAHGSL DDLKLFTESV KRWDLSLVDQ MPQQMKICFV
GFYNTFNDIA KEGRERQGRD VLGYIQNVWK VQLEAYTKEA EWSEAKYVPS FNEYIENASV
SIALGTVVLI SALFTGEVLT DEVLSKIDRE SRFLQLMGLT GRLVNDTKTY QAERGQGEVA
SAIQCYMKDH PKISEEEALQ HVYSVMENAL EELNREFVNN KIPDIYKRLV FETARIMQLF
YMQGDGLTLS HDMEIKEHVK NCLFQPVA
