TPSD8_ABIGR
ID TPSD8_ABIGR Reviewed; 630 AA.
AC Q9M7D1;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Beta-phellandrene synthase, chloroplastic;
DE EC=4.2.3.52;
DE AltName: Full=(-)-(4S)-beta-phellandrene synthase;
DE AltName: Full=Agg-Bphe;
DE Flags: Precursor;
GN Name=ag8; Synonyms=agc8;
OS Abies grandis (Grand fir) (Pinus grandis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Abies.
OX NCBI_TaxID=46611;
RN [1]
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 (Abies
RT grandis).";
RL Arch. Biochem. Biophys. 368:232-243(1999).
RN [2]
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 analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:4126-4133(1998).
RN [3]
RP GENE FAMILY, NOMENCLATURE, AND FUNCTION.
RX PubMed=11404343; DOI=10.1093/genetics/158.2.811;
RA Trapp S.C., Croteau R.B.;
RT "Genomic organization of plant terpene synthases and molecular evolutionary
RT implications.";
RL Genetics 158:811-832(2001).
CC -!- FUNCTION: Converts geranyl diphosphate to four products with (-)-(4S)-
CC beta-phellandrene (52%) as the major olefin, and lesser amounts of (-)-
CC (1S,5S)-beta-pinene (34%), (-)-1S,5S-alpha-pinene (8.5%), and (-)-(4S)-
CC limonene (6%). 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:
CC Reaction=(2E)-geranyl diphosphate = (-)-beta-phellandrene +
CC diphosphate; Xref=Rhea:RHEA:25492, ChEBI:CHEBI:129,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.52;
CC Evidence={ECO:0000269|PubMed:10441373};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={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 for
CC the catalytic activity, presumably through binding to Mg(2+).
CC -!- MISCELLANEOUS: The conserved 62-Arg-Arg-63 motif may play a role in the
CC isomerization step of the terpenoid cyclization reaction sequence.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily.
CC {ECO:0000305}.
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DR EMBL; AF139205; AAF61453.1; -; mRNA.
DR AlphaFoldDB; Q9M7D1; -.
DR SMR; Q9M7D1; -.
DR PRIDE; Q9M7D1; -.
DR KEGG; ag:AAF61453; -.
DR BioCyc; MetaCyc:AG8-MON; -.
DR BRENDA; 4.2.3.52; 2.
DR UniPathway; UPA00924; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR CDD; cd00684; Terpene_cyclase_plant_C1; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR Gene3D; 1.50.10.130; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR034741; Terpene_cyclase-like_1_C.
DR InterPro; IPR044814; Terpene_cyclase_plant_C1.
DR InterPro; IPR001906; Terpene_synth_N.
DR InterPro; IPR036965; Terpene_synth_N_sf.
DR InterPro; IPR005630; Terpene_synthase_metal-bd.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR Pfam; PF01397; Terpene_synth; 1.
DR Pfam; PF03936; Terpene_synth_C; 1.
DR SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 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..48
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 49..630
FT /note="Beta-phellandrene synthase, chloroplastic"
FT /id="PRO_0000033630"
FT MOTIF 381..385
FT /note="DDXXD motif"
FT BINDING 381
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 381
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 385
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 385
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 533
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 630 AA; 72784 MW; B8E4374B262FF2D1 CRC64;
MALVSSAPKS CLHKSLIRST HHELKPLRRT IPTLGMCRRG KSFTPSVSMS LTTAVSDDGL
QRRIGDYHSN LWDDDFIQSL STPYGEPSYR ERAEKLIGEV KEMFNSMPSE DGESMSPLND
LIERLWMVDS VERLGIDRHF KKEIKSALDY VYSYWNEKGI GCGRDSVFPD VNSTASGFRT
LRLHGYSVSS EVLKVFQDQN GQFAFSPSTK ERDIRTVLNL YRASFIAFPG EKVMEEAEIF
SSRYLKEAVQ KIPVSSLSQE IDYTLEYGWH TNMPRLETRN YLDVFGHPTS PWLKKKRTQY
LDSEKLLELA KLEFNIFHSL QQKELQYLSR WWIHSGLPEL TFGRHRHVEY YTLSSCIATE
PKHSAFRLGF AKTCHLITVL DDIYDTFGTM DEIELFNEAV RRWNPSEKER LPEYMKEIYM
ALYEALTDMA REAEKTQGRD TLNYARKAWE VYLDSYTQEA KWIASGYLPT FEEYLENAKV
SSGHRAAALT PLLTLDVPLP DDVLKGIDFP SRFNDLASSF LRLRGDTRCY KADRDRGEEA
SSISCYMKDN PGLTEEDALN HINAMINDII KELNWELLKP DSNIPMTARK HAYEITRAFH
QLYKYRDGFS VATQETKSLV RRTVLEPVPL
