Q5SBP2 (FES_OCIBA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
(-)-endo-fenchol synthase, chloroplastic
EC=4.2.3.10

Gene names

Name:

FES

Organism

Ocimum basilicum (Sweet basil)

Taxonomic identifier

39350 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Lamiales › Lamiaceae › Nepetoideae › Ocimeae › Ocimum

Protein attributes

Sequence length	598 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Monoterpene synthase that catalyzes the formation of fenchol from geranyl diphosphate. Ref.1
Catalytic activity	Geranyl diphosphate = (-)-endo-fenchol + diphosphate. Ref.1
Cofactor	Binds 3 magnesium or manganese ions per subunit By similarity.
Pathway	Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular location	Plastid › chloroplast Potential.
Domain	The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg2+.
Sequence similarities	Belongs to the terpene synthase family.

Ontologies

Keywords
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	Magnesium Metal-binding
Molecular function	Lyase
Gene Ontology (GO)
Biological_process	terpenoid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	(-)-endo-fenchol synthase activity Inferred from electronic annotation. Source: EC 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
	Transit peptide	1 – 34	34	Chloroplast Potential
	Chain	35 – 598	564	(-)-endo-fenchol synthase, chloroplastic		PRO_0000399249
Regions
	Motif	351 – 355	5	DDXXD motif
Sites
	Metal binding	351	1	Magnesium or manganese 1 By similarity
	Metal binding	351	1	Magnesium or manganese 2 By similarity
	Metal binding	355	1	Magnesium or manganese 1 By similarity
	Metal binding	355	1	Magnesium or manganese 2 By similarity
	Metal binding	495	1	Magnesium or manganese 3 By similarity
	Metal binding	499	1	Magnesium or manganese 3 By similarity
	Metal binding	503	1	Magnesium or manganese 3 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5SBP2 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: B3393F62A43B7264	FASTA	598	69,865
	10 20 30 40 50 60 MWSTISISMN VAILKKPLNF LHNSNNKASN PRCVSSTRRR PSCPLQLDVE PRRSGNYQPS 70 80 90 100 110 120 AWDFNYIQSL NNNHSKEERH LQGKAKLIEE VKMLLEQEMA AVQQLEFIED LKNLGLSYLF 130 140 150 160 170 180 QDEIKIILNS IYNHHKCFHN NHQQRTDENA DLYFVALGFR LFRQHGFKVS QEVFDCFKNE 190 200 210 220 230 240 EGSDFIPNLA EDTKGLLQLY EASYLVRQDE DTLEMARQFS TKILQKKVEE KMIEENLLSW 250 260 270 280 290 300 TCHSLELPLH WRVQRIEAKW FLDAYASKPD MNPIIFELAK LEFNIAQALQ QGELKDLSRW 310 320 330 340 350 360 WNDTGIAEKL PFARDRIVEA HYWAIGTLEP YQYRYQRSLI AKIIALTTVV DDVYDVYGTL 370 380 390 400 410 420 DEPQLFTDAI RRWDIESINQ LPHYLQLCYL AIYNFVSELA YDIFRDKGFN SLPYLHKSWL 430 440 450 460 470 480 DLVEAYFLEA KWFHSGYTPT LEEYLNNSKM TITCPAIVSE IYFAFANSID KTEVESVYKY 490 500 510 520 530 540 HDILYLSGML LRLPDDLGTT TFEMKRGDVA KAIQCYMKEH NASEEEAREH IRFLMREAWK 550 560 570 580 590 QMNTAAAANN CPFVNDFVVG AASLGRVANF VYVEGDGFGV QHSKIHQQMA ELLFYPYQ

References

[1]

"The biochemical and molecular basis for the divergent patterns in the biosynthesis of terpenes and phenylpropenes in the peltate glands of three cultivars of basil." Iijima Y., Davidovich-Rikanati R., Fridman E., Gang D.R., Bar E., Lewinsohn E., Pichersky E. Plant Physiol. 136:3724-3736(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY693648 mRNA. Translation: AAV63790.1.
3D structure databases
ProteinModelPortal	Q5SBP2.
SMR	Q5SBP2. Positions 52-597.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-15443.
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

FES_OCIBA

Accession

Primary (citable) accession number: Q5SBP2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
Last sequence update:	December 21, 2004
Last modified:	May 1, 2013
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program