ID   MIBS_SACEN              Reviewed;         354 AA.
AC   A4FG19;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=2-methylisoborneol synthase;
DE            Short=2-MIB synthase;
DE            EC=4.2.3.118;
GN   OrderedLocusNames=SACE_3722;
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS   NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC   2338;
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA   Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
RN   [2]
RP   FUNCTION IN 2-METHYLISOBORNEOL BIOSYNTHESIS, AND PATHWAY.
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:0000305|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;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
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; AM420293; CAM02994.1; -; Genomic_DNA.
DR   RefSeq; WP_011874125.1; NZ_PDBV01000001.1.
DR   AlphaFoldDB; A4FG19; -.
DR   SMR; A4FG19; -.
DR   STRING; 405948.SACE_3722; -.
DR   EnsemblBacteria; CAM02994; CAM02994; SACE_3722.
DR   KEGG; sen:SACE_3722; -.
DR   eggNOG; COG3170; Bacteria.
DR   HOGENOM; CLU_047127_0_0_11; -.
DR   OMA; VDGNHHW; -.
DR   OrthoDB; 1869158at2; -.
DR   Proteomes; UP000006728; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0010333; F:terpene synthase activity; ISS: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; Reference proteome.
FT   CHAIN           1..354
FT                   /note="2-methylisoborneol synthase"
FT                   /id="PRO_0000403383"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         113
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         114
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         118
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         264
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         268
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         272
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   354 AA;  39136 MW;  27D53B700D9AFCAC CRC64;
     MIELIGHETP VPSQQQHTGG VRGTSACTPP GVGERTTVLY CPPPPPERPE VAAEINRRVV
     VWMQGLGLGG EDNVAGVYKH DPGRGITLCH PGSQDVERMT AAGKMIVAET AVDDYFCETN
     SRRDANDQTI GPNLSLAQSA IDAPRLTPDL QALWNKCRDD HPVLRAQHEA FGDLERISSP
     AQAQRVRHDI AQLYLGYNAE NGWRLLNRLP PVWQYLANRQ MNSFRPCLNL TDALDGYELA
     PQLYAHPLVQ DCTARATLIA TLYNDLASCE REIREHGLPF NLPAVIAAEE RIALDEAFVR
     ACEIHNELIQ ALEEATGHAA SALADPALSR YLTGLWSWLA GSRHWHFTTA RHRA