MIBS_STRLS
ID MIBS_STRLS Reviewed; 481 AA.
AC D3KYU2;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=2-methylisoborneol synthase;
DE Short=2-MIB synthase;
DE EC=4.2.3.118;
GN Name=tpc;
OS Streptomyces lasalocidi (Streptomyces lasaliensis).
OG Plasmid pKSL.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=324833;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31180 / DSM 41442 / NRRL 3382 / X-537;
RA Oikawa H., Tsuda M., Migita A.;
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND PATHWAY.
RC STRAIN=ATCC 31180 / DSM 41442 / NRRL 3382 / X-537;
RX PubMed=18492804; DOI=10.1073/pnas.0802312105;
RA Komatsu M., Tsuda M., Omura S., Oikawa H., Ikeda H.;
RT "Identification and functional analysis of genes controlling biosynthesis
RT of 2-methylisoborneol.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7422-7427(2008).
CC -!- FUNCTION: Catalyzes the cyclization of 2-methylgeranyl diphosphate (2-
CC MeGPP) to 2-methylisoborneol (2-MIB), which likely involves the
CC intermediacy of 2-methyllinalyl diphosphate.
CC {ECO:0000269|PubMed:18492804}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-2-methylgeranyl diphosphate + H2O = 2-methylisoborneol +
CC diphosphate; Xref=Rhea:RHEA:32571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:61984, ChEBI:CHEBI:61987;
CC EC=4.2.3.118; Evidence={ECO:0000269|PubMed:18492804};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:18492804};
CC -!- MISCELLANEOUS: 2-MIB is a volatile organic compound that has an
CC unusually low odor threshold. Together with geosmin, methylisoborneol
CC is responsible for the characteristic smell of moist soil as well as
CC unpleasant taste and odor episodes associated with public water
CC supplies and contamination of various foodstuffs, including fish, wine,
CC and beer.
CC -!- SIMILARITY: Belongs to the terpene synthase family. 2-methylisoborneol
CC synthase subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB547324; BAI77523.1; -; Genomic_DNA.
DR AlphaFoldDB; D3KYU2; -.
DR SMR; D3KYU2; -.
DR KEGG; ag:BAI77523; -.
DR BRENDA; 4.2.3.118; 12665.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR GO; GO:0042214; P:terpene metabolic process; IDA:UniProtKB.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR034686; Terpene_cyclase-like_2.
DR SFLD; SFLDG01020; Terpene_Cyclase_Like_2; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding; Plasmid.
FT CHAIN 1..481
FT /note="2-methylisoborneol synthase"
FT /id="PRO_0000403385"
FT REGION 1..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..104
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 238
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 386
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 390
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 481 AA; 51628 MW; 78723282CBA5A7EA CRC64;
MPDSGSLGPP TSLPEQPPAP PATAPDAPAA TVTDRPVTSS VAHFLAGLHP PVTRPSSPPS
PSMPPASSNP SSPPSSSMPP ASWAPPSPLS PPAPSLPPTS PPATAPETSA ATGSDSVVRR
VPVGPTGLGT TALSLARRQA AVPPDAVPAP SGPSAEGPVV PGLYHHPIPE PDPVRVAEVS
RRIKRWAEDE VRLYPEEWEG QFDGFSVGRY MVACHPDAPT VDHLMLATRL MVAENAVDDC
YCEDHGGSPV GLGGRLLLAH TALDHLHTTA EYAPEWSESL GSDAPRRAYR SAMDHFVRAA
TPSQADRYRH DMARLHLGYL AEAAWAETGH VPEVCEYLAM RQFNNFRPCP TITDTVGGYE
LPADLHARPD MQRVIALAGN ATTIVNDLYS YTKELDSPGR HLNLPVVIAE REHLSDRDAY
LKAVEVHNEL MHAFEAAAAE LAADCPVPAV LRFLRGVAAW VDGNHDWHRT NTYRYSLPDF
W