BPHS4_PICSI
ID BPHS4_PICSI Reviewed; 624 AA.
AC F2XFA1;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=(-)-beta-phellandrene synthase 4, chloroplastic {ECO:0000303|PubMed:21385377};
DE EC=4.2.3.52 {ECO:0000269|PubMed:21385377};
DE AltName: Full=Terpene synthase TPS-Phel-4 {ECO:0000303|PubMed:21385377};
DE Short=PsTPS-Phel-4 {ECO:0000303|PubMed:21385377};
DE Flags: Precursor;
GN Name=TPS-Phel-4 {ECO:0000303|PubMed:21385377};
OS Picea sitchensis (Sitka spruce) (Pinus sitchensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX NCBI_TaxID=3332;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, PATHWAY, AND GENE
RP FAMILY.
RC STRAIN=cv. Gb2-229;
RX PubMed=21385377; DOI=10.1186/1471-2229-11-43;
RA Keeling C.I., Weisshaar S., Ralph S.G., Jancsik S., Hamberger B.,
RA Dullat H.K., Bohlmann J.;
RT "Transcriptome mining, functional characterization, and phylogeny of a
RT large terpene synthase gene family in spruce (Picea spp.).";
RL BMC Plant Biol. 11:43-43(2011).
CC -!- FUNCTION: Terpene synthase (TPS) involved in the biosynthesis of
CC monoterpene natural products included in conifer oleoresin secretions
CC and volatile emissions; these compounds contribute to biotic and
CC abiotic stress defense against herbivores and pathogens
CC (PubMed:21385377). Catalyzes the conversion of (2E)-geranyl diphosphate
CC (GPP) to (-)-beta-phellandrene (PubMed:21385377).
CC {ECO:0000269|PubMed:21385377}.
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:21385377};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:A0A1C9J6A7};
CC -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis.
CC {ECO:0000269|PubMed:21385377}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
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 {ECO:0000250|UniProtKB:A0A1C9J6A7}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily.
CC {ECO:0000305}.
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DR EMBL; HQ426159; ADZ45503.1; -; mRNA.
DR UniPathway; UPA00924; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IDA:UniProtKB.
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 GO; GO:0010597; P:green leaf volatile biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016099; P:monoterpenoid biosynthetic process; IDA:UniProtKB.
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; Metal-binding; Plastid; Transit peptide.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 49..624
FT /note="(-)-beta-phellandrene synthase 4, chloroplastic"
FT /id="PRO_0000454407"
FT REGION 41..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 375..379
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT COMPBIAS 45..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 375
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 375
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 379
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 379
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 527
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 624 AA; 71408 MW; 511189B41F6636F7 CRC64;
MAIVSSVPLA SKSCLHKSLI SSIHKLKPFC RTIPTLGMSR PGKSVMPSMS MSSPVSDDGV
QRRTGGYHSN LWNDDIIQFL STPYGEPAYR ERGERLIDEV KNMFNSISME DVEFSPLNDL
IQRLWIVDSV ERLGIDRHFK NEIKSTLDYV YSYWTQKGIG CGIESVVPDL NSTALGLRTL
RLHGYPVSAE VLKHFQNQNG QFACSPSETE GEMRSIVNLY RASLIAFPGE KVMEEAEIFS
TKYLKEALQK IPVSSLSREI GDVLEQDWHT NLPRLEARNY IDVFGQDTKD TKLYMKTEKL
LELAKLEFNI FQSLQKTELD SLLRWWKDSG FHHITFSRHL HVEYYTLASC IAFEPQHSRF
RLGFAKACHV ITILDDMYDV FGTIDELELF TAQIKRWDPS ATDCLPKYMK RMYMILYDMV
NEMSREAETA QGRDTLNYAR QAWEDFIDSY MQEAKWIATG YLPTFDEYFE NGKVSSGHRV
AALQPILTMD IPFPHDILKE VDFPSKLNDL ASAILRLRGD TRCYKADRAR GEEASCISCY
MKDNPGATEE DALSHINAVI NDVIKGLNWE LLNPNSSVPI SSKKHVFDVS RALHYGYKYR
DGYSVSNIET KSLVMRTLLE SVPF
