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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
 
 
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