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Protein

Bifunctional abietadiene synthase, chloroplastic

Gene

AS

Organism
Abies grandis (Grand fir) (Pinus grandis)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Protein has several cofactor binding sites:
  • Mg2+By similarityNote: Binds 3 Mg2+ ions per subunit.By similarity
  • K(+)

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

    Pathway:ioleoresin biosynthesis

    This protein is involved in the pathway oleoresin biosynthesis, which is part of Terpene metabolism.
    View all proteins of this organism that are known to be involved in the pathway oleoresin biosynthesis and in Terpene metabolism.

    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

    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase, Lyase

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-12822.
    BRENDAi4.2.3.132. 2.
    4.2.3.18. 2.
    UniPathwayiUPA00924.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional abietadiene synthase, chloroplastic
    Alternative name(s):
    (-)-abieta-7(8),13(14)-diene synthase
    Abietadiene cyclase
    Short name:
    AgAS
    Agggabi
    Including the following 2 domains:
    Abietadiene synthase (EC:4.2.3.18)
    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

    GO - Cellular componenti

    Complete GO annotation...

    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 – 868798Bifunctional abietadiene 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 – 12918Combined sources
    Helixi139 – 1457Combined sources
    Beta strandi155 – 1595Combined sources
    Helixi160 – 1689Combined sources
    Beta strandi179 – 1813Combined sources
    Helixi184 – 20017Combined sources
    Helixi205 – 21915Combined sources
    Helixi220 – 2245Combined sources
    Helixi234 – 24714Combined sources
    Helixi257 – 27014Combined sources
    Helixi275 – 2806Combined sources
    Helixi284 – 2918Combined sources
    Turni293 – 2953Combined sources
    Helixi298 – 3025Combined sources
    Helixi315 – 32511Combined sources
    Helixi328 – 34114Combined sources
    Helixi352 – 36514Combined sources
    Helixi369 – 3724Combined sources
    Helixi373 – 38412Combined sources
    Helixi403 – 41513Combined sources
    Helixi422 – 4287Combined sources
    Helixi446 – 45611Combined sources
    Helixi464 – 48017Combined sources
    Turni481 – 4833Combined sources
    Beta strandi492 – 4943Combined sources
    Helixi496 – 50510Combined sources
    Helixi508 – 5103Combined sources
    Helixi513 – 52311Combined sources
    Beta strandi530 – 5367Combined sources
    Turni539 – 5413Combined sources
    Helixi544 – 57431Combined sources
    Turni575 – 5784Combined sources
    Beta strandi581 – 5833Combined sources
    Helixi587 – 59711Combined sources
    Helixi601 – 6033Combined sources
    Helixi604 – 62421Combined sources
    Helixi630 – 64213Combined sources
    Beta strandi644 – 6474Combined sources
    Helixi648 – 6503Combined sources
    Helixi653 – 67725Combined sources
    Helixi682 – 70423Combined sources
    Helixi711 – 72111Combined sources
    Helixi724 – 7318Combined sources
    Beta strandi735 – 7373Combined sources
    Helixi741 – 7444Combined sources
    Turni745 – 7473Combined sources
    Helixi752 – 77625Combined sources
    Helixi782 – 7898Combined sources
    Helixi795 – 81925Combined sources
    Helixi824 – 84017Combined sources
    Helixi851 – 86313Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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 motifCurated
    Motifi621 – 6255DDXXD motifCurated

    Domaini

    The Asp-Xaa-Asp-Asp (DXDD) motif is important for the catalytic activity in the class II active site relevant for the cyclization of GGPP. The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity in the class I active site, presumably through binding to Mg2+.Curated

    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.
    InterProiIPR008949. Isoprenoid_synthase_dom.
    IPR001906. Terpene_synth_N.
    IPR005630. Terpene_synthase_metal-bd.
    IPR008930. Terpenoid_cyclase/PrenylTrfase.
    [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

            10         20         30         40         50
    MAMPSSSLSS QIPTAAHHLT ANAQSIPHFS TTLNAGSSAS KRRSLYLRWG
    60 70 80 90 100
    KGSNKIIACV GEGGATSVPY QSAEKNDSLS SSTLVKREFP PGFWKDDLID
    110 120 130 140 150
    SLTSSHKVAA SDEKRIETLI SEIKNMFRCM GYGETNPSAY DTAWVARIPA
    160 170 180 190 200
    VDGSDNPHFP ETVEWILQNQ LKDGSWGEGF YFLAYDRILA TLACIITLTL
    210 220 230 240 250
    WRTGETQVQK GIEFFRTQAG KMEDEADSHR PSGFEIVFPA MLKEAKILGL
    260 270 280 290 300
    DLPYDLPFLK QIIEKREAKL KRIPTDVLYA LPTTLLYSLE GLQEIVDWQK
    310 320 330 340 350
    IMKLQSKDGS FLSSPASTAA VFMRTGNKKC LDFLNFVLKK FGNHVPCHYP
    360 370 380 390 400
    LDLFERLWAV DTVERLGIDR HFKEEIKEAL DYVYSHWDER GIGWARENPV
    410 420 430 440 450
    PDIDDTAMGL RILRLHGYNV SSDVLKTFRD ENGEFFCFLG QTQRGVTDML
    460 470 480 490 500
    NVNRCSHVSF PGETIMEEAK LCTERYLRNA LENVDAFDKW AFKKNIRGEV
    510 520 530 540 550
    EYALKYPWHK SMPRLEARSY IENYGPDDVW LGKTVYMMPY ISNEKYLELA
    560 570 580 590 600
    KLDFNKVQSI HQTELQDLRR WWKSSGFTDL NFTRERVTEI YFSPASFIFE
    610 620 630 640 650
    PEFSKCREVY TKTSNFTVIL DDLYDAHGSL DDLKLFTESV KRWDLSLVDQ
    660 670 680 690 700
    MPQQMKICFV GFYNTFNDIA KEGRERQGRD VLGYIQNVWK VQLEAYTKEA
    710 720 730 740 750
    EWSEAKYVPS FNEYIENASV SIALGTVVLI SALFTGEVLT DEVLSKIDRE
    760 770 780 790 800
    SRFLQLMGLT GRLVNDTKTY QAERGQGEVA SAIQCYMKDH PKISEEEALQ
    810 820 830 840 850
    HVYSVMENAL EELNREFVNN KIPDIYKRLV FETARIMQLF YMQGDGLTLS
    860
    HDMEIKEHVK NCLFQPVA
    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:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U50768 mRNA. Translation: AAB05407.1.
    AF326516 Genomic DNA. Translation: AAK83563.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U50768 mRNA. Translation: AAB05407.1.
    AF326516 Genomic DNA. Translation: AAK83563.1.

    3D structure databases

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

    Proteomic databases

    PRIDEiQ38710.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00924.
    BioCyciMetaCyc:MONOMER-12822.
    BRENDAi4.2.3.132. 2.
    4.2.3.18. 2.

    Family and domain databases

    Gene3Di1.10.600.10. 1 hit.
    1.50.10.20. 1 hit.
    1.50.30.10. 1 hit.
    InterProiIPR008949. Isoprenoid_synthase_dom.
    IPR001906. Terpene_synth_N.
    IPR005630. Terpene_synthase_metal-bd.
    IPR008930. Terpenoid_cyclase/PrenylTrfase.
    [Graphical view]
    PfamiPF01397. Terpene_synth. 1 hit.
    PF03936. Terpene_synth_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF48239. SSF48239. 3 hits.
    SSF48576. SSF48576. 1 hit.
    ProtoNetiSearch...

    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: April 1, 2015
    This is version 87 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.