PIN_CHAFM
ID PIN_CHAFM Reviewed; 628 AA.
AC C3RSF5;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Alpha pinene synthase, chloroplastic {ECO:0000303|Ref.1};
DE Short=Cf-Pin {ECO:0000303|Ref.1};
DE EC=4.2.3.- {ECO:0000269|Ref.1};
DE Flags: Precursor;
GN Name=Pin {ECO:0000303|Ref.1};
OS Chamaecyparis formosensis (Formosan cypress) (Cupressus formosensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers II; Cupressales; Cupressaceae;
OC Chamaecyparis.
OX NCBI_TaxID=187461;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX DOI=10.1515/HF.2009.019;
RA Chu F.-H., Kuo P.-M., Chen Y.-R., Wang S.-Y.;
RT "Cloning and characterization of alpha-pinene synthase from Chamaecyparis
RT formosensis Matsum.";
RL Holzforschung 63:69-74(2009).
CC -!- FUNCTION: Monoterpene synthase involved in the biosynthesis of volatile
CC compounds (Ref.1). Mediates the conversion of (2E)-geranyl diphosphate
CC (GPP) into alpha-pinene (Ref.1). {ECO:0000269|Ref.1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = alpha-pinene + diphosphate;
CC Xref=Rhea:RHEA:25662, ChEBI:CHEBI:33019, ChEBI:CHEBI:36740,
CC ChEBI:CHEBI:58057; Evidence={ECO:0000269|Ref.1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25663;
CC Evidence={ECO:0000269|Ref.1};
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: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|Ref.1}.
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:Q40577}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC {ECO:0000305}.
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DR EMBL; EU099434; ABW80964.1; -; mRNA.
DR UniPathway; UPA00213; -.
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; IDA:UniProtKB.
DR GO; GO:0046248; P:alpha-pinene biosynthetic process; IDA:UniProtKB.
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..46
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 47..628
FT /note="Alpha pinene synthase, chloroplastic"
FT /id="PRO_0000454950"
FT MOTIF 381..385
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 381
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 381
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 385
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 385
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 532
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 628 AA; 72300 MW; 8827B5A4B390C896 CRC64;
MSLGCITPLA SAMVGPKLVR PLIHHNPLFH HKPLNRPYLQ TKIPLRSRVA QNPINMALIT
TDEGITRRIG NHHPNLWDDD FIQSLSKAYE APSYGERAEK LIKDVRDMFN ALPLHSSSAD
DLIQHLSLVD SVERLGIDRH FQNEIKTALD YVYRYWSDAG IGCGRESTHA DLNTTALGFR
ILRLHRYSVS SDVLQQFVLR DGPFLDSNNQ PNEDDIKNIL NLFRGSLIAF PGENVLDDAK
SFTMTYLKQV LPKISNLNLS REIKFNLEYG WHTNVPRLEA RTYIDIYGED SSWASKSINN
IFYTKLLELA KLDFNIIQSL QQQELQILSR WWMESDLGKL DFARHRHVEY YLWAATGCIE
PKYSAFRIGF AKLSALVTYL DDMYDTYDFD EIKIFTKAIK RWDASIIKGL PEFMKVAFKA
FDEAVKDMAQ EAKKTQGRDT LDYARKAWEV YIDAYMKEAE WLATGYMPSL EEYLENGKVS
AGSRVVTLQP ILSLDVPLSD DILKEIDYPS RFDELLCLTL RLRGDTRTFK AEADRGEVVS
CITCYMKDHP GSNEEDALNY LNSLIDERLK ELNWEYLKTD NVPIISKGNA YNLSKGLQLL
YKERDGFTVF SIETKNFIYR MMIGSIPI
