PINS_FRAVE
ID PINS_FRAVE Reviewed; 556 AA.
AC O23945;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=(-)-alpha-pinene synthase;
DE Short=FvPINS;
DE EC=4.2.3.119;
OS Fragaria vesca (Woodland strawberry) (Potentilla vesca).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Rosoideae; Potentilleae; Fragariinae;
OC Fragaria.
OX NCBI_TaxID=57918;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Aharoni A., Jongsma M.A., Verhoeven H.A., Bouwmeester H.J.;
RT "Isoprenoid synthases.";
RL Patent number WO02064764, 22-AUG-2002.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=15522848; DOI=10.1105/tpc.104.023895;
RA Aharoni A., Giri A.P., Verstappen F.W., Bertea C.M., Sevenier R., Sun Z.,
RA Jongsma M.A., Schwab W., Bouwmeester H.J.;
RT "Gain and loss of fruit flavor compounds produced by wild and cultivated
RT strawberry species.";
RL Plant Cell 16:3110-3131(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 209-556, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RX PubMed=10092188; DOI=10.1023/a:1006179928312;
RA Nam Y.W., Tichit L., Leperlier M., Cuerq B., Marty I., Lelievre J.M.;
RT "Isolation and characterization of mRNAs differentially expressed during
RT ripening of wild strawberry (Fragaria vesca L.) fruits.";
RL Plant Mol. Biol. 39:629-636(1999).
CC -!- FUNCTION: Monoterpene synthase catalyzing the production of (-)-alpha-
CC pinene, beta-phellandrene and beta-myrcene as the major products.
CC Unable to use farnesyl diphosphate as substrate. Exclusively expressed
CC in the fruit of wild strawberries. Not detected in cultivated
CC varieties. {ECO:0000269|PubMed:15522848}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = (1S,5S)-alpha-pinene + diphosphate;
CC Xref=Rhea:RHEA:25488, ChEBI:CHEBI:28660, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.119;
CC Evidence={ECO:0000269|PubMed:15522848};
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 -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15522848}.
CC -!- TISSUE SPECIFICITY: Expressed in ripe fruits and roots. Not detected in
CC vegetative tissues. {ECO:0000269|PubMed:10092188,
CC ECO:0000269|PubMed:15522848}.
CC -!- DEVELOPMENTAL STAGE: Expressed during fruit ripening.
CC {ECO:0000269|PubMed:10092188}.
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 -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC {ECO:0000305}.
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DR EMBL; AX529025; CAD57092.1; -; Unassigned_DNA.
DR EMBL; AJ001452; CAA04773.1; -; mRNA.
DR AlphaFoldDB; O23945; -.
DR SMR; O23945; -.
DR PRIDE; O23945; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0005829; C:cytosol; 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 Cytoplasm; Lyase; Magnesium; Manganese; Metal-binding.
FT CHAIN 1..556
FT /note="(-)-alpha-pinene synthase"
FT /id="PRO_0000407983"
FT MOTIF 309..313
FT /note="DDXXD motif"
FT BINDING 309
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 313
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 313
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 453
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT CONFLICT 303
FT /note="E -> K (in Ref. 3; CAA04773)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="M -> I (in Ref. 3; CAA04773)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="I -> R (in Ref. 3; CAA04773)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 556 AA; 64450 MW; 7E2A584C1C33041A CRC64;
MPVHATPAAE SQIISKPEVV RRTANFKPSV WGDRFANYAE DIITQTQMQE QVEELKQVVR
KEVFTNAADD SSHQLKLIDE IQRLGVAYHF ESEIDQALER IHETYQDIHD GGDLYNVALR
FRLLRRHGYN VSCDVFNKFK DTNGDYKKSL VTDLSGMLSF YEAAHLRVHG EKLLEEALVF
TTTHLQSASA KSSLLKTQIT EAVERPLLKT MERLGARRYM SIYQDEASYS ENLLKLAKLD
FNVVQCLHKK ELSDILRWYK ELDFARRMPF ARDRIVELFF WIAGIYFEPE YVFGRHILTK
LIEITTVMDD MYDAFGTFEE LVILTEAIDR WDASCMDQLP DYMQPFYITL LDVIDEVEEE
LTKQGRSYRI HYAKEIMKNQ ARLYFAEAIW FHEGCTPKMD GYMRVAASSV GNTMLSVVSL
VGMGDIITKF EFEWLTNEPK ILRASNTIFR LMDDIAGYKF EKERGHVASS IDCYMNEYGV
SEQETIDIFN KRIVDSWKDI NEEFLRPTAA PVPVLNRVLN LTRVVDLLYK RGDAFTHVGK
LMKDCIAAMF IDPVPL
