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Q38710

- TPSDV_ABIGR

UniProt

Q38710 - TPSDV_ABIGR

Protein

Abietadiene synthase, chloroplastic

Gene

AS

Organism
Abies grandis (Grand fir) (Pinus grandis)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Involved in defensive oleoresin formation in conifers in response to insect attack or other injury. Involved in diterpene (C20) olefins biosynthesis. Bifunctional enzyme that catalyzes two sequential cyclizations of geranylgeranyl diphosphate (GGPP) to abietadiene. The copalyl diphosphate (CPP) intermediate diffuses freely between the 2 active sites in the enzyme. Changes in reaction pH, but not salt concentration, influence the relative proportion of the major products of the enzyme, abitadiene, levopimaradiene and neoabitadiene.7 Publications

    Catalytic activityi

    Geranylgeranyl diphosphate = (+)-copalyl diphosphate.
    +-copalyl diphosphate = abieta-7,13-diene + diphosphate.
    +-copalyl diphosphate = neoabietadiene + diphosphate.

    Cofactori

    Binds 3 magnesium ions per subunit.By similarity
    Potassium.

    Enzyme regulationi

    Not inhibited by 13-cyclopropylidene or 16-methylidenegeranylgeranyl diphosphate. The copalyl diphosphate synthase activity is not susceptible to magnesium-dependent inhibition.1 Publication

    Kineticsi

    1. KM=3 µM for GGPP (in presence of magnesium)2 Publications
    2. KM=20 µM for GGPP (in absence of magnesium)2 Publications
    3. KM=0.4 µM for CPP (in presence of magnesium)2 Publications
    4. KM=10 µM for CPP (in absence of magnesium)2 Publications

    pH dependencei

    Optimum pH is 7.2 with GGPP as substrate and 8.7 with CPP as substrate.2 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi621 – 6211Magnesium 1By similarity
    Metal bindingi621 – 6211Magnesium 2By similarity
    Metal bindingi625 – 6251Magnesium 1By similarity
    Metal bindingi625 – 6251Magnesium 2By similarity
    Metal bindingi765 – 7651Magnesium 3By similarity
    Metal bindingi769 – 7691Magnesium 3By similarity
    Metal bindingi773 – 7731Magnesium 3By similarity

    GO - Molecular functioni

    1. abietadiene synthase activity Source: UniProtKB-EC
    2. copalyl diphosphate synthase activity Source: UniProtKB-EC
    3. magnesium ion binding Source: InterPro
    4. terpene synthase activity Source: InterPro

    Keywords - Molecular functioni

    Isomerase, Lyase

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-12822.
    BRENDAi4.2.3.18. 2.
    UniPathwayiUPA00924.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Abietadiene synthase, chloroplastic
    Alternative name(s):
    (-)-abieta-7(8),13(14)-diene synthase
    Abietadiene cyclase
    Short name:
    AgAS
    Agggabi
    Including the following 2 domains:
    Alternative name(s):
    Neoabietadiene synthase (EC:4.2.3.132)
    Copalyl diphosphate synthase (EC:5.5.1.12)
    Gene namesi
    Name:AS
    Synonyms:ac22, ag22
    OrganismiAbies grandis (Grand fir) (Pinus grandis)
    Taxonomic identifieri46611 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaPinidaePinalesPinaceaeAbies

    Subcellular locationi

    Plastidchloroplast By similarity

    GO - Cellular componenti

    1. chloroplast Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chloroplast, Plastid

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi86 – 861K → A: No effect on CPP binding, but decreased abietadiene synthase activity; when associated with A-87. 1 Publication
    Mutagenesisi87 – 871R → A: No effect on CPP binding, but decreased abietadiene synthase activity; when associated with A-86. 1 Publication
    Mutagenesisi356 – 3561R → A: No effect on abietadiene synthase activity, but strongly reduced copalyl diphosphate synthase activity. 1 Publication
    Mutagenesisi356 – 3561R → H: Increased Mg(2+) inhibition; when associated with A-621. 1 Publication
    Mutagenesisi358 – 3581W → A: Decreased copalyl diphosphate synthase activity. 1 Publication
    Mutagenesisi361 – 3611D → A: No effect on GGPP binding, but decreased copalyl diphosphate synthase activity. 1 Publication
    Mutagenesisi365 – 3651R → A: No effect on GGPP binding, but decreased copalyl diphosphate synthase activity. 1 Publication
    Mutagenesisi402 – 4021D → A, E or N: No effect on GGPP binding, but decreased copalyl diphosphate synthase activity. 1 Publication
    Mutagenesisi404 – 4041D → A, E or N: No effect on GGPP binding, but loss of copalyl diphosphate synthase activity. 2 Publications
    Mutagenesisi405 – 4051D → A, E or N: No effect on GGPP binding, but decreased copalyl diphosphate synthase activity. 1 Publication
    Mutagenesisi411 – 4111R → A: No effect on GGPP binding, but slightly decreased copalyl diphosphate synthase activity. 1 Publication
    Mutagenesisi451 – 4511N → A: No effect on abietadiene synthase activity, but strongly reduced copalyl diphosphate synthase activity. 1 Publication
    Mutagenesisi454 – 4541R → A: No effect on GGPP binding, but decreased copalyl diphosphate synthase activity. 1 Publication
    Mutagenesisi499 – 4991E → A: No effect on GGPP binding, but decreased copalyl diphosphate synthase activity. 1 Publication
    Mutagenesisi520 – 5201Y → A: No effect on GGPP binding, but slightly decreased copalyl diphosphate synthase activity. 1 Publication
    Mutagenesisi584 – 5841R → A: No or small effect on substrate binding, but strongly decreases abietadiene synthase activity. 1 Publication
    Mutagenesisi586 – 5861R → A: No or small effect on substrate binding, but strongly decreases abietadiene synthase activity. 1 Publication
    Mutagenesisi589 – 5891E → A: Lower substrate binding and strong decrease of abietadiene synthase activity. 1 Publication
    Mutagenesisi617 – 6171T → A: Increased production of abietadiene at the expense of levopimaradiene. 1 Publication
    Mutagenesisi621 – 6211D → A: Loss of abietadiene synthase activity. Increased Mg(2+) inhibition; when associated with H-356. 3 Publications
    Mutagenesisi625 – 6251D → A: No or small effect on substrate binding, but strongly decreases abietadiene synthase activity. 1 Publication
    Mutagenesisi699 – 6991E → A: No or small effect on substrate binding, but strongly decreases abietadiene synthase activity. 1 Publication
    Mutagenesisi721 – 7211S → A: Lower substrate binding and strong decrease of abietadiene synthase activity. 1 Publication
    Mutagenesisi723 – 7231A → S: Produces pimaradienes instead of abietadienes. 1 Publication
    Mutagenesisi727 – 7271V → T: No effect. 1 Publication
    Mutagenesisi762 – 7621R → A: No or small effect on substrate binding, but strongly decreases abietadiene synthase activity. 1 Publication
    Mutagenesisi765 – 7651N → A: Abolishes the conversion of CPP to abietadiene; produces only sandaracopimaradiene. 1 Publication
    Mutagenesisi766 – 7661D → A: No or small effect on substrate binding, but strongly decreases abietadiene synthase activity. 1 Publication
    Mutagenesisi769 – 7691T → A: Increased production of neoabietadiene at the expense of both levopimaradiene and abietadiene. 1 Publication
    Mutagenesisi773 – 7731E → A: Increased production of neoabietadiene. 1 Publication
    Mutagenesisi778 – 7781E → A: No or small effect on substrate binding, but strongly decreases abietadiene synthase activity. 1 Publication
    Mutagenesisi841 – 8411Y → F: No or small effect on substrate binding, but strongly decreases abietadiene synthase activity. 1 Publication
    Mutagenesisi845 – 8451D → A: No or small effect on substrate binding, but strongly decreases abietadiene synthase activity. 1 Publication
    Mutagenesisi848 – 8481T → A: No or small effect on substrate binding, but strongly decreases abietadiene synthase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 7070ChloroplastSequence AnalysisAdd
    BLAST
    Chaini71 – 868798Abietadiene synthase, chloroplasticPRO_0000033634Add
    BLAST

    Post-translational modificationi

    The N-terminus is blocked.

    Proteomic databases

    PRIDEiQ38710.

    Expressioni

    Inductioni

    By wounding.1 Publication

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    Secondary structure

    1
    868
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi112 – 12918
    Helixi139 – 1457
    Beta strandi155 – 1595
    Helixi160 – 1689
    Beta strandi179 – 1813
    Helixi184 – 20017
    Helixi205 – 21915
    Helixi220 – 2245
    Helixi234 – 24714
    Helixi257 – 27014
    Helixi275 – 2806
    Helixi284 – 2918
    Turni293 – 2953
    Helixi298 – 3025
    Helixi315 – 32511
    Helixi328 – 34114
    Helixi352 – 36514
    Helixi369 – 3724
    Helixi373 – 38412
    Helixi403 – 41513
    Helixi422 – 4287
    Helixi446 – 45611
    Helixi464 – 48017
    Turni481 – 4833
    Beta strandi492 – 4943
    Helixi496 – 50510
    Helixi508 – 5103
    Helixi513 – 52311
    Beta strandi530 – 5367
    Turni539 – 5413
    Helixi544 – 57431
    Turni575 – 5784
    Beta strandi581 – 5833
    Helixi587 – 59711
    Helixi601 – 6033
    Helixi604 – 62421
    Helixi630 – 64213
    Beta strandi644 – 6474
    Helixi648 – 6503
    Helixi653 – 67725
    Helixi682 – 70423
    Helixi711 – 72111
    Helixi724 – 7318
    Beta strandi735 – 7373
    Helixi741 – 7444
    Turni745 – 7473
    Helixi752 – 77625
    Helixi782 – 7898
    Helixi795 – 81925
    Helixi824 – 84017
    Helixi851 – 86313

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3S9VX-ray2.30A/B/C/D85-868[»]
    ProteinModelPortaliQ38710.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi402 – 4054DXDD motif
    Motifi621 – 6255DDXXD motif

    Domaini

    The Asp-Xaa-Asp-Asp (DXDD) and the Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motifs are important for the catalytic activities, presumably through binding to Mg2+.

    Sequence similaritiesi

    Belongs to the terpene synthase family. Tpsd subfamily.Curated

    Keywords - Domaini

    Transit peptide

    Family and domain databases

    Gene3Di1.10.600.10. 1 hit.
    1.50.10.20. 1 hit.
    1.50.30.10. 1 hit.
    InterProiIPR001906. Terpene_synth_N.
    IPR005630. Terpene_synthase_metal-bd.
    IPR008930. Terpenoid_cyclase/PrenylTrfase.
    IPR008949. Terpenoid_synth.
    [Graphical view]
    PfamiPF01397. Terpene_synth. 1 hit.
    PF03936. Terpene_synth_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF48239. SSF48239. 3 hits.
    SSF48576. SSF48576. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q38710-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAMPSSSLSS QIPTAAHHLT ANAQSIPHFS TTLNAGSSAS KRRSLYLRWG    50
    KGSNKIIACV GEGGATSVPY QSAEKNDSLS SSTLVKREFP PGFWKDDLID 100
    SLTSSHKVAA SDEKRIETLI SEIKNMFRCM GYGETNPSAY DTAWVARIPA 150
    VDGSDNPHFP ETVEWILQNQ LKDGSWGEGF YFLAYDRILA TLACIITLTL 200
    WRTGETQVQK GIEFFRTQAG KMEDEADSHR PSGFEIVFPA MLKEAKILGL 250
    DLPYDLPFLK QIIEKREAKL KRIPTDVLYA LPTTLLYSLE GLQEIVDWQK 300
    IMKLQSKDGS FLSSPASTAA VFMRTGNKKC LDFLNFVLKK FGNHVPCHYP 350
    LDLFERLWAV DTVERLGIDR HFKEEIKEAL DYVYSHWDER GIGWARENPV 400
    PDIDDTAMGL RILRLHGYNV SSDVLKTFRD ENGEFFCFLG QTQRGVTDML 450
    NVNRCSHVSF PGETIMEEAK LCTERYLRNA LENVDAFDKW AFKKNIRGEV 500
    EYALKYPWHK SMPRLEARSY IENYGPDDVW LGKTVYMMPY ISNEKYLELA 550
    KLDFNKVQSI HQTELQDLRR WWKSSGFTDL NFTRERVTEI YFSPASFIFE 600
    PEFSKCREVY TKTSNFTVIL DDLYDAHGSL DDLKLFTESV KRWDLSLVDQ 650
    MPQQMKICFV GFYNTFNDIA KEGRERQGRD VLGYIQNVWK VQLEAYTKEA 700
    EWSEAKYVPS FNEYIENASV SIALGTVVLI SALFTGEVLT DEVLSKIDRE 750
    SRFLQLMGLT GRLVNDTKTY QAERGQGEVA SAIQCYMKDH PKISEEEALQ 800
    HVYSVMENAL EELNREFVNN KIPDIYKRLV FETARIMQLF YMQGDGLTLS 850
    HDMEIKEHVK NCLFQPVA 868
    Length:868
    Mass (Da):99,536
    Last modified:November 1, 1996 - v1
    Checksum:iAD5E79F56B70D25C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti23 – 231A → T in AAK83563. (PubMed:11404343)Curated
    Sequence conflicti214 – 2141F → S in AAK83563. (PubMed:11404343)Curated
    Sequence conflicti297 – 2993DWQ → EWE in AAK83563. (PubMed:11404343)Curated
    Sequence conflicti557 – 5571V → L in AAK83563. (PubMed:11404343)Curated
    Sequence conflicti579 – 5791D → E in AAK83563. (PubMed:11404343)Curated
    Sequence conflicti653 – 6531Q → K in AAK83563. (PubMed:11404343)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U50768 mRNA. Translation: AAB05407.1.
    AF326516 Genomic DNA. Translation: AAK83563.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U50768 mRNA. Translation: AAB05407.1 .
    AF326516 Genomic DNA. Translation: AAK83563.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3S9V X-ray 2.30 A/B/C/D 85-868 [» ]
    ProteinModelPortali Q38710.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q38710.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00924 .
    BioCyci MetaCyc:MONOMER-12822.
    BRENDAi 4.2.3.18. 2.

    Family and domain databases

    Gene3Di 1.10.600.10. 1 hit.
    1.50.10.20. 1 hit.
    1.50.30.10. 1 hit.
    InterProi IPR001906. Terpene_synth_N.
    IPR005630. Terpene_synthase_metal-bd.
    IPR008930. Terpenoid_cyclase/PrenylTrfase.
    IPR008949. Terpenoid_synth.
    [Graphical view ]
    Pfami PF01397. Terpene_synth. 1 hit.
    PF03936. Terpene_synth_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48239. SSF48239. 3 hits.
    SSF48576. SSF48576. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Abietadiene synthase from grand fir (Abies grandis). cDNA isolation, characterization, and bacterial expression of a bifunctional diterpene cyclase involved in resin acid biosynthesis."
      Stoffer Vogel B., Wildung M.R., Vogel G., Croteau R.B.
      J. Biol. Chem. 271:23262-23268(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 148-166; 522-530; 615-625 AND 699-705, INDUCTION.
      Tissue: Stem.
    2. "Genomic organization of plant terpene synthases and molecular evolutionary implications."
      Trapp S.C., Croteau R.B.
      Genetics 158:811-832(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-868, NOMENCLATURE.
    3. "Plant terpenoid synthases: molecular biology and phylogenetic analysis."
      Bohlmann J., Meyer-Gauen G., Croteau R.B.
      Proc. Natl. Acad. Sci. U.S.A. 95:4126-4133(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY, NOMENCLATURE, FUNCTION.
    4. "Abietadiene synthase from grand fir (Abies grandis): characterization and mechanism of action of the 'pseudomature' recombinant enzyme."
      Peters R.J., Flory J.E., Jetter R., Ravn M.M., Lee H.J., Coates R.M., Croteau R.B.
      Biochemistry 39:15592-15602(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    5. "Stereochemistry of the cyclization-rearrangement of (+)-copalyl diphosphate to (-)-abietadiene catalyzed by recombinant abietadiene synthase from Abies grandis."
      Ravn M.M., Coates R.M., Flory J.E., Peters R.J., Croteau R.
      Org. Lett. 2:573-576(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    6. "Bifunctional abietadiene synthase: free diffusive transfer of the (+)-copalyl diphosphate intermediate between two distinct active sites."
      Peters R.J., Ravn M.M., Coates R.M., Croteau R.B.
      J. Am. Chem. Soc. 123:8974-8978(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-404 AND ASP-621, CHARACTERIZATION.
    7. "Abietadiene synthase catalysis: conserved residues involved in protonation-initiated cyclization of geranylgeranyl diphosphate to (+)-copalyl diphosphate."
      Peters R.J., Croteau R.B.
      Biochemistry 41:1836-1842(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, 3D-STRUCTURE MODELING, MUTAGENESIS OF TRP-358; ASP-361; ARG-365; ASP-402; ASP-404; ASP-405; ARG-411; ARG-454; GLU-499 AND TYR-520.
    8. "Abietadiene synthase catalysis: mutational analysis of a prenyl diphosphate ionization-initiated cyclization and rearrangement."
      Peters R.J., Croteau R.B.
      Proc. Natl. Acad. Sci. U.S.A. 99:580-584(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ARG-584; ARG-586; GLU-589; THR-617; ASP-621; ASP-625; GLU-699; SER-721; ARG-762; ASN-765; ASP-766; THR-769; GLU-773; GLU-778; TYR-841; ASP-845 AND THR-848, CHARACTERIZATION.
    9. "Bifunctional abietadiene synthase: mutual structural dependence of the active sites for protonation-initiated and ionization-initiated cyclizations."
      Peters R.J., Carter O.A., Zhang Y., Matthews B.W., Croteau R.B.
      Biochemistry 42:2700-2707(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-86 AND ARG-87.
    10. "A single residue switch converts abietadiene synthase into a pimaradiene specific cyclase."
      Wilderman P.R., Peters R.J.
      J. Am. Chem. Soc. 129:15736-15737(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ALA-723.
    11. "A single residue switch for Mg(2+)-dependent inhibition characterizes plant class II diterpene cyclases from primary and secondary metabolism."
      Mann F.M., Prisic S., Davenport E.K., Determan M.K., Coates R.M., Peters R.J.
      J. Biol. Chem. 285:20558-20563(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ARG-356 AND ASP-621.
    12. "Insights into diterpene cyclization from structure of bifunctional abietadiene synthase from Abies grandis."
      Zhou K., Gao Y., Hoy J.A., Mann F.M., Honzatko R.B., Peters R.J.
      J. Biol. Chem. 287:6840-6850(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 85-868, MUTAGENESIS OF ASN-451 AND VAL-727.

    Entry informationi

    Entry nameiTPSDV_ABIGR
    AccessioniPrimary (citable) accession number: Q38710
    Secondary accession number(s): Q94FW1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 12, 2005
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 83 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The abietadiene synthase activity exhibits an absolute dependence on a divalent metal ion cofactor while the copalyl diphosphate synthase activity is not completely dependent.

    Keywords - Technical termi

    3D-structure, Direct protein sequencing, Multifunctional enzyme

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3