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Protein

2-methylisoborneol synthase

Gene

SCO7700

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the cyclization of 2-methylgeranyl diphosphate (2-MeGPP) to 2-methylisoborneol (2-MIB), which likely involves the intermediacy of 2-methyllinalyl diphosphate. Is also able to catalyze the cyclization of geranyl diphosphate (GPP), albeit with much lower efficiency, leading to the formation of a complex mixture of cyclic monoterpenes, consisting of alpha-pinene (6%), beta-pinene (23%), limonene (32%), gamma-terpinene (29%), and delta-terpinene (10%).1 Publication

Catalytic activityi

(E)-2-methylgeranyl diphosphate + H2O = 2-methylisoborneol + diphosphate.1 Publication

Cofactori

Mg2+1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi197 – 1971MagnesiumBy similarity
Metal bindingi198 – 1981MagnesiumBy similarity
Metal bindingi202 – 2021MagnesiumBy similarity
Metal bindingi345 – 3451MagnesiumBy similarity
Metal bindingi349 – 3491MagnesiumBy similarity
Metal bindingi353 – 3531MagnesiumBy similarity

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • terpene synthase activity Source: UniProtKB

GO - Biological processi

  • terpene metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17560.
BRENDAi4.2.3.118. 5998.

Names & Taxonomyi

Protein namesi
Recommended name:
2-methylisoborneol synthase (EC:4.2.3.118)
Short name:
2-MIB synthase
Gene namesi
Ordered Locus Names:SCO7700
ORF Names:SC1A4.08, SCBAC12C8.01
OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Taxonomic identifieri100226 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
Proteomesi
  • UP000001973 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4404402-methylisoborneol synthasePRO_0000205354Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi100226.SCO7700.

Structurei

Secondary structure

1
440
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi132 – 14817Combined sources
Helixi155 – 1573Combined sources
Helixi163 – 17311Combined sources
Helixi180 – 20021Combined sources
Beta strandi204 – 2063Combined sources
Helixi211 – 2199Combined sources
Turni220 – 2223Combined sources
Turni229 – 2313Combined sources
Helixi232 – 2387Combined sources
Helixi243 – 25816Combined sources
Helixi261 – 28626Combined sources
Helixi293 – 30210Combined sources
Beta strandi303 – 3053Combined sources
Turni306 – 3083Combined sources
Helixi309 – 3113Combined sources
Helixi312 – 3165Combined sources
Helixi322 – 3254Combined sources
Helixi328 – 34821Combined sources
Helixi350 – 3534Combined sources
Beta strandi356 – 3583Combined sources
Helixi363 – 3719Combined sources
Helixi375 – 40329Combined sources
Helixi407 – 42923Combined sources
Turni431 – 4333Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3V1VX-ray1.80A29-440[»]
3V1XX-ray1.96A1-440[»]
4LA5X-ray1.85A1-440[»]
4LA6X-ray2.00A1-440[»]
ProteinModelPortaliQ9F1Y6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108QZR. Bacteria.
ENOG4110Y17. LUCA.
HOGENOMiHOG000053689.
InParanoidiQ9F1Y6.
KOiK16218.
OMAiYSLPDFW.
OrthoDBiPOG091H0D9P.

Family and domain databases

Gene3Di1.10.600.10. 1 hit.
InterProiIPR008949. Isoprenoid_synthase_dom.
[Graphical view]
SUPFAMiSSF48576. SSF48576. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9F1Y6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPDSGTLGTP PPEQGPTPPT TLPDVPAPVI PSASVTSAAS DFLAALHPPV
60 70 80 90 100
TVPDPAPPPP PAPAAGNPPD TVTGDSVLQR ILRGPTGPGT TSLAPAVRYG
110 120 130 140 150
RQPGPEAPAS APPAAGRAVP GLYHHPVPEP DPVRVEEVSR RIKRWAEDEV
160 170 180 190 200
QLYPEEWEGQ FDGFSVGRYM VGCHPDAPTV DHLMLATRLM VAENAVDDCY
210 220 230 240 250
CEDHGGSPVG LGGRLLLAHT AIDHFHSTAE YTPTWQASLA ADAPRRAYDS
260 270 280 290 300
AMGYFVRAAT PSQSDRYRHD MARLHLGYLA EGAWAQTGHV PEVWEYLAMR
310 320 330 340 350
QFNNFRPCPT ITDTVGGYEL PADLHARPDM QRVIALAGNA TTIVNDLYSY
360 370 380 390 400
TKELNSPGRH LNLPVVIAER EQLCERDAYL KAVEVHNELQ HSFEAAAADL
410 420 430 440
AEACPLPPVL RFLRGVAAWV DGNHDWHRTN TYRYSLPDFW
Length:440
Mass (Da):47,793
Last modified:March 1, 2001 - v1
Checksum:i0228C9B635F4CBE2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB035202 Genomic DNA. Translation: BAB20433.1.
AL939132 Genomic DNA. Translation: CAD55534.1.
RefSeqiNP_733742.1. NC_003888.3.
WP_011031839.1. NC_003888.3.

Genome annotation databases

EnsemblBacteriaiCAD55534; CAD55534; CAD55534.
GeneIDi1103138.
KEGGisco:SCO7700.
PATRICi23745355. VBIStrCoe124346_7820.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB035202 Genomic DNA. Translation: BAB20433.1.
AL939132 Genomic DNA. Translation: CAD55534.1.
RefSeqiNP_733742.1. NC_003888.3.
WP_011031839.1. NC_003888.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3V1VX-ray1.80A29-440[»]
3V1XX-ray1.96A1-440[»]
4LA5X-ray1.85A1-440[»]
4LA6X-ray2.00A1-440[»]
ProteinModelPortaliQ9F1Y6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi100226.SCO7700.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAD55534; CAD55534; CAD55534.
GeneIDi1103138.
KEGGisco:SCO7700.
PATRICi23745355. VBIStrCoe124346_7820.

Phylogenomic databases

eggNOGiENOG4108QZR. Bacteria.
ENOG4110Y17. LUCA.
HOGENOMiHOG000053689.
InParanoidiQ9F1Y6.
KOiK16218.
OMAiYSLPDFW.
OrthoDBiPOG091H0D9P.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17560.
BRENDAi4.2.3.118. 5998.

Family and domain databases

Gene3Di1.10.600.10. 1 hit.
InterProiIPR008949. Isoprenoid_synthase_dom.
[Graphical view]
SUPFAMiSSF48576. SSF48576. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMIBS_STRCO
AccessioniPrimary (citable) accession number: Q9F1Y6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: March 1, 2001
Last modified: September 7, 2016
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

2-MIB is a volatile organic compound that has an unusually low odor threshold. Together with geosmin, methylisoborneol is responsible for the characteristic smell of moist soil as well as unpleasant taste and odor episodes associated with public water supplies and contamination of various foodstuffs, including fish, wine, and beer.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.