Q675L5 (TPSD2_PICAB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Picea abies (Norway spruce) (Picea excelsa)

Taxonomic identifier

3329 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Coniferophyta › Coniferopsida › Coniferales › Pinaceae › Picea

Protein attributes

Sequence length	867 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Plastid › chloroplast 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 component	Chloroplast Plastid
Domain	Transit peptide
Ligand	Magnesium Metal-binding
Molecular function	Isomerase Lyase
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Cellular_component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	copalyl diphosphate synthase activity Inferred from electronic annotation. Source: 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 68	68	Chloroplast Potential
	Chain	69 – 867	799	Isopimaradiene synthase, chloroplastic		PRO_0000348953
Regions
	Motif	619 – 623	5	DDXXD motif
Sites
	Metal binding	619	1	Magnesium 1 By similarity
	Metal binding	619	1	Magnesium 2 By similarity
	Metal binding	623	1	Magnesium 1 By similarity
	Metal binding	623	1	Magnesium 2 By similarity
	Metal binding	763	1	Magnesium 3 By similarity
	Metal binding	767	1	Magnesium 3 By similarity
	Metal binding	771	1	Magnesium 3 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q675L5 [UniParc]. Last modified November 22, 2005. Version 2. Checksum: 7E27A5BBCC6062D7	FASTA	867	99,203
	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

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
HSSP	HSSP built from PDB template 1HX9 based on UniProtKB Q40577.
ProteinModelPortal	Q675L5.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-12744.
BRENDA	4.2.3.35. 4815.
UniPathway	UPA00924.
Family and domain databases
Gene3D	1.10.600.10. 1 hit. 1.50.30.10. 1 hit.
InterPro	IPR001906. Terpene_synth_N. IPR005630. Terpene_synthase_metal-bd. IPR008930. Terpenoid_cyclase/PrenylTrfase. IPR008949. Terpenoid_synth. [Graphical view]
Pfam	PF01397. Terpene_synth. 1 hit. PF03936. Terpene_synth_C. 1 hit. [Graphical view]
SUPFAM	SSF48239. Terp_cyc_toroid. 2 hits. SSF48576. Terpenoid_synth. 1 hit.
ProtoNet	Search...

Entry information

Entry name

TPSD2_PICAB

Accession

Primary (citable) accession number: Q675L5

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
Last sequence update:	November 22, 2005
Last modified:	May 1, 2013
This is version 45 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program