Q49SP3 (TPSPS_POGCB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Patchoulol synthase Short name=PatTps177 EC=4.2.3.70 Alternative name(s): Alpha-guaiene synthase EC=4.2.3.87 Delta-guaiene synthase EC=4.2.3.93
Organism	Pogostemon cablin (Patchouli) (Mentha cablin)
Taxonomic identifier	28511 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Lamiales › Lamiaceae › Lamioideae › Pogostemoneae › Pogostemon

Protein attributes

Sequence length	552 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the biosynthesis of patchoulol. Produces also at least 13 additional sesquiterpene products, including alpha- and beta-patchoulene, alpha-bulnesene, seychellene, pogostol and alpha-guiaene. Ref.1 Ref.2 Ref.3 Ref.4
Catalytic activity	(2E,6E)-farnesyl diphosphate + H2O = patchoulol + diphosphate. Ref.1 Ref.2 Ref.3 Ref.4 (2E,6E)-farnesyl diphosphate = alpha-guaiene + diphosphate. Ref.1 Ref.2 Ref.3 Ref.4 (2E,6E)-farnesyl diphosphate = delta-guaiene + diphosphate. Ref.1 Ref.2 Ref.3 Ref.4
Cofactor	Magnesium or manganese. Ref.3
Pathway	Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subunit structure	Homodimer. Ref.3
Subcellular location	Cytoplasm Probable.
Domain	The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg2+ By similarity.
Sequence similarities	Belongs to the terpene synthase family.
Biophysicochemical properties	Kinetic parameters: KM=4.45 µM for farnesyl diphosphate Ref.1 Ref.3 pH dependence: Optimum pH is 7.0-7.5. Temperature dependence: Optimum temperature is 40 degrees Celsius.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Magnesium Manganese Metal-binding
Molecular function	Lyase
Gene Ontology (GO)
Biological_process	terpenoid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: InterPro terpene synthase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 552	552	Patchoulol synthase		PRO_0000412251
Regions
	Motif	304 – 308	5	DDXXD motif
Sites
	Metal binding	304	1	Magnesium or manganese 1 By similarity
	Metal binding	304	1	Magnesium or manganese 2 By similarity
	Metal binding	308	1	Magnesium or manganese 1 By similarity
	Metal binding	308	1	Magnesium or manganese 2 By similarity
	Metal binding	457	1	Magnesium or manganese 3 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q49SP3 [UniParc]. Last modified September 13, 2005. Version 1. Checksum: 05533EFBD57B6C75	FASTA	552	64,199
	10 20 30 40 50 60 MELYAQSVGV GAASRPLANF HPCVWGDKFI VYNPQSCQAG EREEAEELKV ELKRELKEAS 70 80 90 100 110 120 DNYMRQLKMV DAIQRLGIDY LFVEDVDEAL KNLFEMFDAF CKNNHDMHAT ALSFRLLRQH 130 140 150 160 170 180 GYRVSCEVFE KFKDGKDGFK VPNEDGAVAV LEFFEATHLR VHGEDVLDNA FDFTRNYLES 190 200 210 220 230 240 VYATLNDPTA KQVHNALNEF SFRRGLPRVE ARKYISIYEQ YASHHKGLLK LAKLDFNLVQ 250 260 270 280 290 300 ALHRRELSED SRWWKTLQVP TKLSFVRDRL VESYFWASGS YFEPNYSVAR MILAKGLAVL 310 320 330 340 350 360 SLMDDVYDAY GTFEELQMFT DAIERWDASC LDKLPDYMKI VYKALLDVFE EVDEELIKLG 370 380 390 400 410 420 APYRAYYGKE AMKYAARAYM EEAQWREQKH KPTTKEYMKL ATKTCGYITL IILSCLGVEE 430 440 450 460 470 480 GIVTKEAFDW VFSRPPFIEA TLIIARLVND ITGHEFEKKR EHVRTAVECY MEEHKVGKQE 490 500 510 520 530 540 VVSEFYNQME SAWKDINEGF LRPVEFPIPL LYLILNSVRT LEVIYKEGDS YTHVGPAMQN 550 IIKQLYLHPV PY

References

[1]	"The diverse sesquiterpene profile of patchouli, Pogostemon cablin, is correlated with a limited number of sesquiterpene synthases." Deguerry F., Pastore L., Wu S., Clark A., Chappell J., Schalk M. Arch. Biochem. Biophys. 454:123-136(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[2]	"Biosynthesis of the sesquiterpene patchoulol from farnesyl pyrophosphate in leaf extracts of Pogostemon cablin (patchouli): mechanistic considerations." Croteau R., Munck S.L., Akoh C.C., Fisk H.J., Satterwhite D.M. Arch. Biochem. Biophys. 256:56-68(1987) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY.
[3]	"Purification and characterization of the sesquiterpene cyclase patchoulol synthase from Pogostemon cablin." Munck S.L., Croteau R. Arch. Biochem. Biophys. 282:58-64(1990) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT.
[4]	"Doubly deuterium-labeled patchouli alcohol from cyclization of singly labeled [2-(2)H(1)]farnesyl diphosphate catalyzed by recombinant patchoulol synthase." Faraldos J.A., Wu S., Chappell J., Coates R.M. J. Am. Chem. Soc. 132:2998-3008(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, 3D-STRUCTURE MODELING.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY508730 mRNA. Translation: AAS86323.1. DQ355151 Genomic DNA. Translation: ABC87816.1.
3D structure databases
ProteinModelPortal	Q49SP3.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-14859.
UniPathway	UPA00213.
Family and domain databases
Gene3D	1.10.600.10. 1 hit. 1.50.30.10. 1 hit.
InterPro	IPR001906. Terpene_synth_N. IPR005630. Terpene_synthase_metal-bd. IPR008930. Terpenoid_cyclase/PrenylTrfase. IPR008949. Terpenoid_synth. [Graphical view]
Pfam	PF01397. Terpene_synth. 1 hit. PF03936. Terpene_synth_C. 1 hit. [Graphical view]
SUPFAM	SSF48239. Terp_cyc_toroid. 1 hit. SSF48576. Terpenoid_synth. 1 hit.
ProtoNet	Search...

Entry information

Entry name

TPSPS_POGCB

Accession

Primary (citable) accession number: Q49SP3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 21, 2011
Last sequence update:	September 13, 2005
Last modified:	May 1, 2013
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program