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Q675L5 (TPSD2_PICAB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Isopimaradiene synthase, chloroplastic
Alternative name(s):
Diterpene synthase
PaTPS-Iso

Including the following 2 domains:

  1. Isopimara-7,15-diene synthase
    Short name=Isopimaradiene synthase
    EC=4.2.3.44
  2. Copalyl diphosphate synthase
    EC=5.5.1.12
Gene names
Name:TPS-ISO
OrganismPicea abies (Norway spruce) (Picea excelsa)
Taxonomic identifier3329 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaPinidaePinalesPinaceaePicea

Protein attributes

Sequence length867 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in defensive oleoresin formation in conifers in response to insect attack or other injury By similarity. Involved in diterpene (C20) olefins biosynthesis. Bifunctional enzyme that catalyzes two sequential cyclizations of geranylgeranyl diphosphate (GGPP) to isopimara-7,15-diene. Ref.1

Catalytic activity

Geranylgeranyl diphosphate = (+)-copalyl diphosphate. Ref.1

+-copalyl diphosphate = isopimara-7,15-diene + diphosphate. Ref.1

Cofactor

Binds 3 magnesium ions per subunit By similarity.

Pathway

Terpene metabolism; oleoresin biosynthesis.

Subcellular location

Plastidchloroplast By similarity.

Domain

The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg2+.

Sequence similarities

Belongs to the terpene synthase family. Tpsd subfamily.

Ontologies

Keywords
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandMagnesium
Metal-binding
   Molecular functionIsomerase
Lyase
   Technical termMultifunctional enzyme
Gene Ontology (GO)
   Cellular_componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncopalyl diphosphate synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

terpene synthase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6868Chloroplast Potential
Chain69 – 867799Isopimaradiene synthase, chloroplastic
PRO_0000348953

Regions

Motif619 – 6235DDXXD motif

Sites

Metal binding6191Magnesium 1 By similarity
Metal binding6191Magnesium 2 By similarity
Metal binding6231Magnesium 1 By similarity
Metal binding6231Magnesium 2 By similarity
Metal binding7631Magnesium 3 By similarity
Metal binding7671Magnesium 3 By similarity
Metal binding7711Magnesium 3 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q675L5 [UniParc].

Last modified November 22, 2005. Version 2.
Checksum: 7E27A5BBCC6062D7

FASTA86799,203
        10         20         30         40         50         60 
MALLSSSLSS QIPTGSHPLT HTQCIPHFST TINAGISAGK PRSFYLRWGK GSNKIIACVG 

        70         80         90        100        110        120 
EGTTSLPYQS AEKTDSLSAP TLVKREFPPG FWKDHVIDSL TSSHKVSAAE EKRMETLISE 

       130        140        150        160        170        180 
IKNIFRSMGY GETNPSAYDT AWVARIPAVD GSEHPEFPET LEWILQNQLK DGSWGEGFYF 

       190        200        210        220        230        240 
LAYDRILATL ACIITLTLWR TGETQIRKGI EFFKTQAGKI EDEADSHRPS GFEIVFPAML 

       250        260        270        280        290        300 
KEAKVLGLDL PYELPFIKQI IEKREAKLER LPTNILYALP TTLLYSLEGL QEIVDWEKII 

       310        320        330        340        350        360 
KLQSKDGSFL TSPASTAAVF MRTGNKKCLE FLNFVLKKFG NHVPCHYPLD LFERLWAVDT 

       370        380        390        400        410        420 
VERLGIDHHF KEEIKDALDY VYSHWDERGI GWARENPIPD IDDTAMGLRI LRLHGYNVSS 

       430        440        450        460        470        480 
DVLKTFRDEN GEFFCFLGQT QRGVTDMLNV NRCSHVAFPG ETIMQEAKLC TERYLRNALE 

       490        500        510        520        530        540 
DVGAFDKWAL KKNIRGEVEY ALKYPWHRSM PRLEARSYIE HYGPNDVWLG KTMYMMPYIS 

       550        560        570        580        590        600 
NLKYLELAKL DFNHVQSLHQ KELRDLRRWW KSSGLSELKF TRERVTEIYF SAASFIFEPE 

       610        620        630        640        650        660 
FATCRDVYTK ISIFTVILDD LYDAHGTLDN LELFSEGVKR WDLSLVDRMP QDMKICFTVL 

       670        680        690        700        710        720 
YNTVNEIAVE GRKRQGRDVL GYIRNVLEIL LAAHTKEAEW SAARYVPSFD EYIENASVSI 

       730        740        750        760        770        780 
SLGTLVLISV LFTGEILTDD VLSKIGRGSR FLQLMGLTGR LVNDTKTYEA ERGQGEVASA 

       790        800        810        820        830        840 
VQCYMKEHPE ISEEEALKHV YTVMENALDE LNREFVNNRD VPDSCRRLVF ETARIMQLFY 

       850        860 
MEGDGLTLSH EMEIKEHVKN CLFQPVA 

« Hide

References

[1]"Functional characterization of nine Norway Spruce TPS genes and evolution of gymnosperm terpene synthases of the TPS-d subfamily."
Martin D.M., Faeldt J., Bohlmann J.
Plant Physiol. 135:1908-1927(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, GENE FAMILY, NOMENCLATURE.
[2]Martin D.M., Keeling C., Bohlmann J.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY473620 mRNA. Translation: AAS47690.2.

3D structure databases

ProteinModelPortalQ675L5.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-12744.
BRENDA4.2.3.35. 4815.
UniPathwayUPA00924.

Family and domain databases

Gene3D1.10.600.10. 1 hit.
1.50.10.20. 1 hit.
1.50.30.10. 1 hit.
InterProIPR001906. Terpene_synth_N.
IPR005630. Terpene_synthase_metal-bd.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
IPR008949. Terpenoid_synth.
[Graphical view]
PfamPF01397. Terpene_synth. 1 hit.
PF03936. Terpene_synth_C. 1 hit.
[Graphical view]
SUPFAMSSF48239. SSF48239. 3 hits.
SSF48576. SSF48576. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTPSD2_PICAB
AccessionPrimary (citable) accession number: Q675L5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: November 22, 2005
Last modified: April 16, 2014
This is version 49 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways