Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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.2 Publications
+-copalyl diphosphate = abieta-7,13-diene + diphosphate.2 Publications
+-copalyl diphosphate = neoabietadiene + diphosphate.2 Publications

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

    Pathwayi: oleoresin 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)DescriptionActionsGraphical viewLength
    Metal bindingi621Magnesium 1By similarity1
    Metal bindingi621Magnesium 2By similarity1
    Metal bindingi625Magnesium 1By similarity1
    Metal bindingi625Magnesium 2By similarity1
    Metal bindingi765Magnesium 3By similarity1
    Metal bindingi769Magnesium 3By similarity1
    Metal bindingi773Magnesium 3By similarity1

    GO - Molecular functioni

    GO - Biological processi

    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:4.2.3.182 Publications)
    Alternative name(s):
    Neoabietadiene synthase (EC:4.2.3.1322 Publications)
    Copalyl diphosphate synthase (EC:5.5.1.122 Publications)
    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)DescriptionActionsGraphical viewLength
    Mutagenesisi86K → A: No effect on CPP binding, but decreased abietadiene synthase activity; when associated with A-87. 1 Publication1
    Mutagenesisi87R → A: No effect on CPP binding, but decreased abietadiene synthase activity; when associated with A-86. 1 Publication1
    Mutagenesisi356R → A: No effect on abietadiene synthase activity, but strongly reduced copalyl diphosphate synthase activity. 1 Publication1
    Mutagenesisi356R → H: Increased Mg(2+) inhibition; when associated with A-621. 1 Publication1
    Mutagenesisi358W → A: Decreased copalyl diphosphate synthase activity. 1 Publication1
    Mutagenesisi361D → A: No effect on GGPP binding, but decreased copalyl diphosphate synthase activity. 1 Publication1
    Mutagenesisi365R → A: No effect on GGPP binding, but decreased copalyl diphosphate synthase activity. 1 Publication1
    Mutagenesisi402D → A, E or N: No effect on GGPP binding, but decreased copalyl diphosphate synthase activity. 1 Publication1
    Mutagenesisi404D → A, E or N: No effect on GGPP binding, but loss of copalyl diphosphate synthase activity. 2 Publications1
    Mutagenesisi405D → A, E or N: No effect on GGPP binding, but decreased copalyl diphosphate synthase activity. 1 Publication1
    Mutagenesisi411R → A: No effect on GGPP binding, but slightly decreased copalyl diphosphate synthase activity. 1 Publication1
    Mutagenesisi451N → A: No effect on abietadiene synthase activity, but strongly reduced copalyl diphosphate synthase activity. 1 Publication1
    Mutagenesisi454R → A: No effect on GGPP binding, but decreased copalyl diphosphate synthase activity. 1 Publication1
    Mutagenesisi499E → A: No effect on GGPP binding, but decreased copalyl diphosphate synthase activity. 1 Publication1
    Mutagenesisi520Y → A: No effect on GGPP binding, but slightly decreased copalyl diphosphate synthase activity. 1 Publication1
    Mutagenesisi584R → A: No or small effect on substrate binding, but strongly decreases abietadiene synthase activity. 1 Publication1
    Mutagenesisi586R → A: No or small effect on substrate binding, but strongly decreases abietadiene synthase activity. 1 Publication1
    Mutagenesisi589E → A: Lower substrate binding and strong decrease of abietadiene synthase activity. 1 Publication1
    Mutagenesisi617T → A: Increased production of abietadiene at the expense of levopimaradiene. 1 Publication1
    Mutagenesisi621D → A: Loss of abietadiene synthase activity. Increased Mg(2+) inhibition; when associated with H-356. 3 Publications1
    Mutagenesisi625D → A: No or small effect on substrate binding, but strongly decreases abietadiene synthase activity. 1 Publication1
    Mutagenesisi699E → A: No or small effect on substrate binding, but strongly decreases abietadiene synthase activity. 1 Publication1
    Mutagenesisi721S → A: Lower substrate binding and strong decrease of abietadiene synthase activity. 1 Publication1
    Mutagenesisi723A → S: Produces pimaradienes instead of abietadienes. 1 Publication1
    Mutagenesisi727V → T: No effect. 1 Publication1
    Mutagenesisi762R → A: No or small effect on substrate binding, but strongly decreases abietadiene synthase activity. 1 Publication1
    Mutagenesisi765N → A: Abolishes the conversion of CPP to abietadiene; produces only sandaracopimaradiene. 1 Publication1
    Mutagenesisi766D → A: No or small effect on substrate binding, but strongly decreases abietadiene synthase activity. 1 Publication1
    Mutagenesisi769T → A: Increased production of neoabietadiene at the expense of both levopimaradiene and abietadiene. 1 Publication1
    Mutagenesisi773E → A: Increased production of neoabietadiene. 1 Publication1
    Mutagenesisi778E → A: No or small effect on substrate binding, but strongly decreases abietadiene synthase activity. 1 Publication1
    Mutagenesisi841Y → F: No or small effect on substrate binding, but strongly decreases abietadiene synthase activity. 1 Publication1
    Mutagenesisi845D → A: No or small effect on substrate binding, but strongly decreases abietadiene synthase activity. 1 Publication1
    Mutagenesisi848T → A: No or small effect on substrate binding, but strongly decreases abietadiene synthase activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Transit peptidei1 – 70ChloroplastSequence analysisAdd BLAST70
    ChainiPRO_000003363471 – 868Bifunctional abietadiene synthase, chloroplasticAdd BLAST798

    Post-translational modificationi

    The N-terminus is blocked.

    Proteomic databases

    PRIDEiQ38710.

    Expressioni

    Inductioni

    By wounding.1 Publication

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    Secondary structure

    1868
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi112 – 129Combined sources18
    Helixi139 – 145Combined sources7
    Beta strandi155 – 159Combined sources5
    Helixi160 – 168Combined sources9
    Beta strandi179 – 181Combined sources3
    Helixi184 – 200Combined sources17
    Helixi205 – 219Combined sources15
    Helixi220 – 224Combined sources5
    Helixi234 – 247Combined sources14
    Helixi257 – 270Combined sources14
    Helixi275 – 280Combined sources6
    Helixi284 – 291Combined sources8
    Turni293 – 295Combined sources3
    Helixi298 – 302Combined sources5
    Helixi315 – 325Combined sources11
    Helixi328 – 341Combined sources14
    Helixi352 – 365Combined sources14
    Helixi369 – 372Combined sources4
    Helixi373 – 384Combined sources12
    Helixi403 – 415Combined sources13
    Helixi422 – 428Combined sources7
    Helixi446 – 456Combined sources11
    Helixi464 – 480Combined sources17
    Turni481 – 483Combined sources3
    Beta strandi492 – 494Combined sources3
    Helixi496 – 505Combined sources10
    Helixi508 – 510Combined sources3
    Helixi513 – 523Combined sources11
    Beta strandi530 – 536Combined sources7
    Turni539 – 541Combined sources3
    Helixi544 – 574Combined sources31
    Turni575 – 578Combined sources4
    Beta strandi581 – 583Combined sources3
    Helixi587 – 597Combined sources11
    Helixi601 – 603Combined sources3
    Helixi604 – 624Combined sources21
    Helixi630 – 642Combined sources13
    Beta strandi644 – 647Combined sources4
    Helixi648 – 650Combined sources3
    Helixi653 – 677Combined sources25
    Helixi682 – 704Combined sources23
    Helixi711 – 721Combined sources11
    Helixi724 – 731Combined sources8
    Beta strandi735 – 737Combined sources3
    Helixi741 – 744Combined sources4
    Turni745 – 747Combined sources3
    Helixi752 – 776Combined sources25
    Helixi782 – 789Combined sources8
    Helixi795 – 819Combined sources25
    Helixi824 – 840Combined sources17
    Helixi851 – 863Combined sources13

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3S9VX-ray2.30A/B/C/D85-868[»]
    ProteinModelPortaliQ38710.
    SMRiQ38710.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Motifi402 – 405DXDD motifCurated4
    Motifi621 – 625DDXXD motifCurated5

    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

    Phylogenomic databases

    KOiK12927.

    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)DescriptionActionsGraphical viewLength
    Sequence conflicti23A → T in AAK83563 (PubMed:11404343).Curated1
    Sequence conflicti214F → S in AAK83563 (PubMed:11404343).Curated1
    Sequence conflicti297 – 299DWQ → EWE in AAK83563 (PubMed:11404343).Curated3
    Sequence conflicti557V → L in AAK83563 (PubMed:11404343).Curated1
    Sequence conflicti579D → E in AAK83563 (PubMed:11404343).Curated1
    Sequence conflicti653Q → K in AAK83563 (PubMed:11404343).Curated1

    Sequence databases

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

    Genome annotation databases

    KEGGiag:AAB05407.

    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3S9VX-ray2.30A/B/C/D85-868[»]
    ProteinModelPortaliQ38710.
    SMRiQ38710.
    ModBaseiSearch...
    MobiDBiSearch...

    Proteomic databases

    PRIDEiQ38710.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:AAB05407.

    Phylogenomic databases

    KOiK12927.

    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...

    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 2, 2016
    This is version 91 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

    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 one 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.