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Q38710

- TPSDV_ABIGR

UniProt

Q38710 - TPSDV_ABIGR

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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

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 Mg(2+) 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

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
Complete GO annotation...

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-KW
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 – 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 – 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 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

        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
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: November 26, 2014
This is version 85 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