TPSPS_POGCB
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 03-AUG-2022, entry version 66.
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. Produces also 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 = diphosphate + patchoulol;
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}.
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DR EMBL; AY508730; AAS86323.1; -; mRNA.
DR EMBL; DQ355151; ABC87816.1; -; Genomic_DNA.
DR AlphaFoldDB; Q49SP3; -.
DR SMR; Q49SP3; -.
DR PRIDE; Q49SP3; -.
DR KEGG; ag:AAS86323; -.
DR BioCyc; MetaCyc:MON-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 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..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
