ID TPSPS_POGCB Reviewed; 552 AA. AC Q49SP3; DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 28-JAN-2026, entry version 75. DE RecName: Full=Patchoulol synthase; DE Short=PatTps177; DE EC=4.2.3.70 {ECO:0000269|PubMed:16970904, ECO:0000269|PubMed:20148554, ECO:0000269|PubMed:2171435, ECO:0000269|PubMed:3038029}; DE AltName: Full=Alpha-guaiene synthase; DE EC=4.2.3.87 {ECO:0000269|PubMed:16970904, ECO:0000269|PubMed:20148554, ECO:0000269|PubMed:2171435}; DE AltName: Full=Delta-guaiene synthase; DE EC=4.2.3.93 {ECO:0000269|PubMed:16970904, ECO:0000269|PubMed:20148554}; OS Pogostemon cablin (Patchouli) (Mentha cablin). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Lamiales; Lamiaceae; Lamioideae; Pogostemoneae; OC Pogostemon. OX NCBI_TaxID=28511; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=16970904; DOI=10.1016/j.abb.2006.08.006; RA Deguerry F., Pastore L., Wu S., Clark A., Chappell J., Schalk M.; RT "The diverse sesquiterpene profile of patchouli, Pogostemon cablin, is RT correlated with a limited number of sesquiterpene synthases."; RL Arch. Biochem. Biophys. 454:123-136(2006). RN [2] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=3038029; DOI=10.1016/0003-9861(87)90425-5; RA Croteau R., Munck S.L., Akoh C.C., Fisk H.J., Satterwhite D.M.; RT "Biosynthesis of the sesquiterpene patchoulol from farnesyl pyrophosphate RT in leaf extracts of Pogostemon cablin (patchouli): mechanistic RT considerations."; RL Arch. Biochem. Biophys. 256:56-68(1987). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND RP SUBUNIT. RX PubMed=2171435; DOI=10.1016/0003-9861(90)90086-e; RA Munck S.L., Croteau R.; RT "Purification and characterization of the sesquiterpene cyclase patchoulol RT synthase from Pogostemon cablin."; RL Arch. Biochem. Biophys. 282:58-64(1990). RN [4] RP FUNCTION, CATALYTIC ACTIVITY, AND 3D-STRUCTURE MODELING. RX PubMed=20148554; DOI=10.1021/ja909251r; RA Faraldos J.A., Wu S., Chappell J., Coates R.M.; RT "Doubly deuterium-labeled patchouli alcohol from cyclization of singly RT labeled [2-(2)H(1)]farnesyl diphosphate catalyzed by recombinant patchoulol RT synthase."; RL J. Am. Chem. Soc. 132:2998-3008(2010). CC -!- FUNCTION: Involved in the biosynthesis of patchoulol. Also produces at CC least 13 additional sesquiterpene products, including alpha- and beta- CC patchoulene, alpha-bulnesene, seychellene, pogostol and alpha-guiaene. CC {ECO:0000269|PubMed:16970904, ECO:0000269|PubMed:20148554, CC ECO:0000269|PubMed:2171435, ECO:0000269|PubMed:3038029}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = patchoulol + diphosphate; CC Xref=Rhea:RHEA:29503, ChEBI:CHEBI:7940, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.70; CC Evidence={ECO:0000269|PubMed:16970904, ECO:0000269|PubMed:20148554, CC ECO:0000269|PubMed:2171435, ECO:0000269|PubMed:3038029}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E,6E)-farnesyl diphosphate = alpha-guaiene + diphosphate; CC Xref=Rhea:RHEA:31807, ChEBI:CHEBI:33019, ChEBI:CHEBI:63443, CC ChEBI:CHEBI:175763; EC=4.2.3.87; CC Evidence={ECO:0000269|PubMed:16970904, ECO:0000269|PubMed:20148554, CC ECO:0000269|PubMed:2171435}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E,6E)-farnesyl diphosphate = delta-guaiene + diphosphate; CC Xref=Rhea:RHEA:31831, ChEBI:CHEBI:33019, ChEBI:CHEBI:63447, CC ChEBI:CHEBI:175763; EC=4.2.3.93; CC Evidence={ECO:0000269|PubMed:16970904, ECO:0000269|PubMed:20148554}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:2171435}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:2171435}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=4.45 uM for farnesyl diphosphate {ECO:0000269|PubMed:16970904, CC ECO:0000269|PubMed:2171435}; CC pH dependence: CC Optimum pH is 7.0-7.5. {ECO:0000269|PubMed:16970904, CC ECO:0000269|PubMed:2171435}; CC Temperature dependence: CC Optimum temperature is 40 degrees Celsius. CC {ECO:0000269|PubMed:16970904, ECO:0000269|PubMed:2171435}; CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:2171435}. 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 {ECO:0000250}. CC -!- SIMILARITY: Belongs to the terpene synthase family. {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; AY508730; AAS86323.1; -; mRNA. DR EMBL; DQ355151; ABC87816.1; -; Genomic_DNA. DR AlphaFoldDB; Q49SP3; -. DR SMR; Q49SP3; -. DR KEGG; ag:AAS86323; -. DR BioCyc; MetaCyc:MONOMER-14859; -. DR BRENDA; 4.2.3.70; 9724. DR BRENDA; 4.2.3.87; 9724. DR UniPathway; UPA00213; -. DR GO; GO:0005737; C:cytoplasm; 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 GO; GO:0051762; P:sesquiterpene biosynthetic process; IEA:UniProtKB-ARBA. DR CDD; cd00684; Terpene_cyclase_plant_C1; 1. DR FunFam; 1.10.600.10:FF:000007; Isoprene synthase, chloroplastic; 1. DR FunFam; 1.50.10.130:FF:000001; Isoprene synthase, chloroplastic; 1. DR Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 1. DR Gene3D; 1.50.10.130; Terpene synthase, N-terminal domain; 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; IPR050148; Terpene_synthase-like. DR InterPro; IPR005630; Terpene_synthase_metal-bd. DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase. DR PANTHER; PTHR31225:SF251; (-)-GERMACRENE D SYNTHASE-LIKE ISOFORM X2; 1. DR PANTHER; PTHR31225; OS04G0344100 PROTEIN-RELATED; 1. DR Pfam; PF01397; Terpene_synth; 1. DR Pfam; PF03936; Terpene_synth_C; 1. DR SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1. DR SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1. DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1. DR SUPFAM; SSF48576; Terpenoid synthases; 1. PE 1: Evidence at protein level; KW Cytoplasm; Lyase; Magnesium; Manganese; Metal-binding. FT CHAIN 1..552 FT /note="Patchoulol synthase" FT /id="PRO_0000412251" FT MOTIF 304..308 FT /note="DDXXD motif" FT BINDING 304 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 304 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 308 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 308 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 457 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000250" SQ SEQUENCE 552 AA; 64199 MW; 05533EFBD57B6C75 CRC64; MELYAQSVGV GAASRPLANF HPCVWGDKFI VYNPQSCQAG EREEAEELKV ELKRELKEAS DNYMRQLKMV DAIQRLGIDY LFVEDVDEAL KNLFEMFDAF CKNNHDMHAT ALSFRLLRQH GYRVSCEVFE KFKDGKDGFK VPNEDGAVAV LEFFEATHLR VHGEDVLDNA FDFTRNYLES VYATLNDPTA KQVHNALNEF SFRRGLPRVE ARKYISIYEQ YASHHKGLLK LAKLDFNLVQ ALHRRELSED SRWWKTLQVP TKLSFVRDRL VESYFWASGS YFEPNYSVAR MILAKGLAVL SLMDDVYDAY GTFEELQMFT DAIERWDASC LDKLPDYMKI VYKALLDVFE EVDEELIKLG APYRAYYGKE AMKYAARAYM EEAQWREQKH KPTTKEYMKL ATKTCGYITL IILSCLGVEE GIVTKEAFDW VFSRPPFIEA TLIIARLVND ITGHEFEKKR EHVRTAVECY MEEHKVGKQE VVSEFYNQME SAWKDINEGF LRPVEFPIPL LYLILNSVRT LEVIYKEGDS YTHVGPAMQN IIKQLYLHPV PY //