ID TPSD6_ABIGR Reviewed; 618 AA. AC Q948Z0; DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 29-OCT-2014, entry version 62. DE RecName: Full=Camphene synthase, chloroplastic; DE EC=4.2.3.117; DE AltName: Full=(-)-(1S,4R)-camphene synthase; DE AltName: Full=Agg-cam; DE Flags: Precursor; GN Name=ag6; Synonyms=AG6.5; OS Abies grandis (Grand fir) (Pinus grandis). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Pinidae; Pinales; Pinaceae; Abies. OX NCBI_TaxID=46611; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=9268308; DOI=10.1074/jbc.272.35.21784; RA Bohlmann J., Steele C.L., Croteau R.B.; RT "Monoterpene synthases from grand fir (Abies grandis). cDNA isolation, RT characterization, and functional expression of myrcene synthase, (-)- RT (4S)-limonene synthase, and (-)-(1S,5S)-pinene synthase."; RL J. Biol. Chem. 272:21784-21792(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY. RC TISSUE=Stem; RX PubMed=10441373; DOI=10.1006/abbi.1999.1332; RA Bohlmann J., Phillips M., Ramachandiran V., Katoh S., Croteau R.B.; RT "cDNA cloning, characterization, and functional expression of four new RT monoterpene synthase members of the Tpsd gene family from grand fir RT (Abies grandis)."; RL Arch. Biochem. Biophys. 368:232-243(1999). RN [3] RP GENE FAMILY, NOMENCLATURE, AND FUNCTION. RX PubMed=9539701; DOI=10.1073/pnas.95.8.4126; RA Bohlmann J., Meyer-Gauen G., Croteau R.B.; RT "Plant terpenoid synthases: molecular biology and phylogenetic RT analysis."; RL Proc. Natl. Acad. Sci. U.S.A. 95:4126-4133(1998). RN [4] RP GENE FAMILY, NOMENCLATURE, AND FUNCTION. RX PubMed=11404343; RA Trapp S.C., Croteau R.B.; RT "Genomic organization of plant terpene synthases and molecular RT evolutionary implications."; RL Genetics 158:811-832(2001). CC -!- FUNCTION: Involved in defensive oleoresin formation in conifers in CC response to insect attack or other injury. Involved in monoterpene CC (C10) olefins biosynthesis. {ECO:0000269|PubMed:10441373, CC ECO:0000269|PubMed:11404343, ECO:0000269|PubMed:9539701}. CC -!- CATALYTIC ACTIVITY: Geranyl-diphosphate = (-)-camphene + CC diphosphate. {ECO:0000269|PubMed:10441373}. CC -!- COFACTOR: Binds 3 magnesium or manganese ions per subunit. CC {ECO:0000250}. CC -!- COFACTOR: Potassium. {ECO:0000250}. CC -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}. CC -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important CC for the catalytic activity, presumably through binding to Mg(2+). CC -!- MISCELLANEOUS: The conserved 59-Arg-Arg-60 motif may play a role CC in the isomerization step of the terpenoid cyclization reaction CC sequence. CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsd CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U87910; AAB70707.1; -; mRNA. DR ProteinModelPortal; Q948Z0; -. DR BioCyc; MetaCyc:AG6-MONOMER; -. DR UniPathway; UPA00924; -. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro. DR Gene3D; 1.10.600.10; -; 1. DR Gene3D; 1.50.30.10; -; 1. DR InterPro; IPR001906; Terpene_synth_N. DR InterPro; IPR005630; Terpene_synthase_metal-bd. DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase. DR InterPro; IPR008949; Terpenoid_synth. DR Pfam; PF01397; Terpene_synth; 1. DR Pfam; PF03936; Terpene_synth_C; 1. DR SUPFAM; SSF48239; SSF48239; 1. DR SUPFAM; SSF48576; SSF48576; 1. PE 1: Evidence at protein level; KW Chloroplast; Lyase; Magnesium; Manganese; Metal-binding; Plastid; KW Transit peptide. FT TRANSIT 1 51 Chloroplast. {ECO:0000255}. FT CHAIN 52 618 Camphene synthase, chloroplastic. FT /FTId=PRO_0000033629. FT MOTIF 369 373 DDXXD motif. FT METAL 369 369 Magnesium or manganese 1. {ECO:0000250}. FT METAL 369 369 Magnesium or manganese 2. {ECO:0000250}. FT METAL 373 373 Magnesium or manganese 1. {ECO:0000250}. FT METAL 373 373 Magnesium or manganese 2. {ECO:0000250}. FT METAL 521 521 Magnesium or manganese 3. {ECO:0000250}. SQ SEQUENCE 618 AA; 70750 MW; B07B5185CE5C4CE1 CRC64; MALLSITPLV SRSCLSSSHE IKALRRTIPT LGICRPGKSV AHSINMCLTS VASTDSVQRR VGNYHSNLWD DDFIQSLIST PYGAPDYRER ADRLIGEVKD IMFNFKSLED GGNDLLQRLL LVDDVERLGI DRHFKKEIKT ALDYVNSYWN EKGIGCGRES VVTDLNSTAL GLRTLRLHGY TVSSDVLNVF KDKNGQFSST ANIQIEGEIR GVLNLFRASL VAFPGEKVMD EAETFSTKYL REALQKIPAS SILSLEIRDV LEYGWHTNLP RLEARNYMDV FGQHTKNKNA AEKLLELAKL EFNIFHSLQE RELKHVSRWW KDSGSPEMTF CRHRHVEYYA LASCIAFEPQ HSGFRLGFTK MSHLITVLDD MYDVFGTVDE LELFTATIKR WDPSAMECLP EYMKGVYMMV YHTVNEMARV AEKAQGRDTL NYARQAWEAC FDSYMQEAKW IATGYLPTFE EYLENGKVSS AHRPCALQPI LTLDIPFPDH ILKEVDFPSK LNDLICIILR LRGDTRCYKA DRARGEEASS ISCYMKDNPG LTEEDALNHI NFMIRDAIRE LNWELLKPDN SVPITSKKHA FDISRVWHHG YRYRDGYSFA NVETKSLVMR TVIEPVPL //