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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)DescriptionActionsGraphical viewLength
Metal bindingi197MagnesiumBy similarity1
Metal bindingi198MagnesiumBy similarity1
Metal bindingi202MagnesiumBy similarity1
Metal bindingi345MagnesiumBy similarity1
Metal bindingi349MagnesiumBy similarity1
Metal bindingi353MagnesiumBy similarity1

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)DescriptionActionsGraphical viewLength
ChainiPRO_00002053541 – 4402-methylisoborneol synthaseAdd BLAST440

Interactioni

Protein-protein interaction databases

STRINGi100226.SCO7700.

Structurei

Secondary structure

1440
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi132 – 148Combined sources17
Helixi155 – 157Combined sources3
Helixi163 – 173Combined sources11
Helixi180 – 200Combined sources21
Beta strandi204 – 206Combined sources3
Helixi211 – 219Combined sources9
Turni220 – 222Combined sources3
Turni229 – 231Combined sources3
Helixi232 – 238Combined sources7
Helixi243 – 258Combined sources16
Helixi261 – 286Combined sources26
Helixi293 – 302Combined sources10
Beta strandi303 – 305Combined sources3
Turni306 – 308Combined sources3
Helixi309 – 311Combined sources3
Helixi312 – 316Combined sources5
Helixi322 – 325Combined sources4
Helixi328 – 348Combined sources21
Helixi350 – 353Combined sources4
Beta strandi356 – 358Combined sources3
Helixi363 – 371Combined sources9
Helixi375 – 403Combined sources29
Helixi407 – 429Combined sources23
Turni431 – 433Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3V1VX-ray1.80A29-440[»]
3V1XX-ray1.96A1-440[»]
4LA5X-ray1.85A1-440[»]
4LA6X-ray2.00A1-440[»]
ProteinModelPortaliQ9F1Y6.
SMRiQ9F1Y6.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3V1VX-ray1.80A29-440[»]
3V1XX-ray1.96A1-440[»]
4LA5X-ray1.85A1-440[»]
4LA6X-ray2.00A1-440[»]
ProteinModelPortaliQ9F1Y6.
SMRiQ9F1Y6.
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: November 2, 2016
This is version 79 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.