ID   PT5_PINTA               Reviewed;         574 AA.
AC   Q84KL5;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Alpha-farnesene synthase;
DE            EC=4.2.3.46;
GN   Name=PT5;
OS   Pinus taeda (Loblolly pine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Pinus.
OX   NCBI_TaxID=3352;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=12623076; DOI=10.1016/s0003-9861(02)00746-4;
RA   Phillips M.A., Wildung M.R., Williams D.C., Hyatt D.C., Croteau R.;
RT   "cDNA isolation, functional expression, and characterization of (+)-alpha-
RT   pinene synthase and (-)-alpha-pinene synthase from loblolly pine (Pinus
RT   taeda): stereocontrol in pinene biosynthesis.";
RL   Arch. Biochem. Biophys. 411:267-276(2003).
CC   -!- FUNCTION: Involved in sesquiterpene (C15) biosynthesis. The major
CC       product is alpha-farnesene. {ECO:0000269|PubMed:12623076}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = (3E,6E)-alpha-farnesene +
CC         diphosphate; Xref=Rhea:RHEA:27421, ChEBI:CHEBI:10280,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.46;
CC         Evidence={ECO:0000269|PubMed:12623076};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 3 Mn(2+) ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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. Tpsd subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF543528; AAO61226.1; -; mRNA.
DR   AlphaFoldDB; Q84KL5; -.
DR   SMR; Q84KL5; -.
DR   UniPathway; UPA00924; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052578; F:alpha-farnesene synthase activity; IEA:RHEA.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0010334; F:sesquiterpene synthase activity; IDA:UniProtKB.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR   GO; GO:0045338; P:farnesyl diphosphate metabolic 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   Cytoplasm; Lyase; Magnesium; Manganese; Metal-binding.
FT   CHAIN           1..574
FT                   /note="Alpha-farnesene synthase"
FT                   /id="PRO_0000419234"
FT   MOTIF           326..330
FT                   /note="DDXXD motif"
FT   BINDING         326
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         326
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         330
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         330
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         478
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   574 AA;  65941 MW;  26746BAE32ACF19A CRC64;
     MSSLAVDDAE RRVGDYHPNL WDDALIQSLS TPYGASPYRD VAEKLIGEIK EMFASISIED
     GDDEICYFLQ RLWMIDNVER LGISRHFENE IKAAMEDVYS RHWSDKGIAC GRHSVVADLN
     STALAFRTLR LHGYSVCSDV FKIFQDQKGE FACSADQTEG EIKGILNLLR ASLIAFPGER
     ILQEAEIFAT TYLKEALPKI QGSRLSQEIE YVLEYGWLTD LPRLETRNYI EVLAEEITPY
     FKKPCMAVEK LLKLAKIEFN LFHSLQQTEL KHLSRWWKDS GFAQLTFTRH RHVEFYTLAS
     CIAMEPKHSA FRLGFAKLCY LGIVLDDIYD TYGKMEELEL FTAAIKRWDT STTECLPEYM
     KGVYMAFYDC VNEMARQAEK TQGWDTLDYA RKTWEALIDA FMEEAKWISS GYVPTFQKYL
     DNGKVSFGYR AATLQPILTL DIPLPLHILQ EIDFPSSFND LASSILRLRG DICGYQAERS
     RGEQASSISC YMKDNPGSTE EDALSHVNAM IGDKIPEFNW EFMKPSKAPI SSKKYAFDIL
     RAFYHLYKYR DGFSIAKIET KKLVMRTVLD PVPM