MIBS_STRCO
ID MIBS_STRCO Reviewed; 440 AA.
AC Q9F1Y6;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=2-methylisoborneol synthase;
DE Short=2-MIB synthase;
DE EC=4.2.3.118;
GN OrderedLocusNames=SCO7700; ORFNames=SC1A4.08, SCBAC12C8.01;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A3(2) / 1147;
RA Watanabe M., Kawamoto S., Ochi K.;
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, KINETIC STUDIES, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=A3(2) / NRRL B-16638;
RX PubMed=18563898; DOI=10.1021/ja803639g;
RA Wang C.M., Cane D.E.;
RT "Biochemistry and molecular genetics of the biosynthesis of the earthy
RT odorant methylisoborneol in Streptomyces coelicolor.";
RL J. Am. Chem. Soc. 130:8908-8909(2008).
RN [4]
RP ERRATUM OF PUBMED:18563898.
RX DOI=10.1021/ja104306p;
RA Wang C.M., Cane D.E.;
RL J. Am. Chem. Soc. 132:9509-9509(2010).
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. Is also able to catalyze
CC the cyclization of geranyl diphosphate (GPP), albeit with much lower
CC efficiency, leading to the formation of a complex mixture of cyclic
CC monoterpenes, consisting of alpha-pinene (6%), beta-pinene (23%),
CC limonene (32%), gamma-terpinene (29%), and delta-terpinene (10%).
CC {ECO:0000269|PubMed:18563898}.
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:18563898};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:18563898};
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}.
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DR EMBL; AB035202; BAB20433.1; -; Genomic_DNA.
DR EMBL; AL939132; CAD55534.1; -; Genomic_DNA.
DR RefSeq; NP_733742.1; NC_003888.3.
DR RefSeq; WP_011031839.1; NZ_VNID01000005.1.
DR PDB; 3V1V; X-ray; 1.80 A; A=29-440.
DR PDB; 3V1X; X-ray; 1.96 A; A=1-440.
DR PDB; 4LA5; X-ray; 1.85 A; A=1-440.
DR PDB; 4LA6; X-ray; 2.00 A; A=1-440.
DR PDBsum; 3V1V; -.
DR PDBsum; 3V1X; -.
DR PDBsum; 4LA5; -.
DR PDBsum; 4LA6; -.
DR AlphaFoldDB; Q9F1Y6; -.
DR SMR; Q9F1Y6; -.
DR STRING; 100226.SCO7700; -.
DR DNASU; 1103138; -.
DR GeneID; 1103138; -.
DR KEGG; sco:SCO7700; -.
DR PATRIC; fig|100226.15.peg.7820; -.
DR eggNOG; COG3170; Bacteria.
DR HOGENOM; CLU_047127_0_0_11; -.
DR InParanoid; Q9F1Y6; -.
DR OMA; VDGNHHW; -.
DR BioCyc; MetaCyc:MON-17560; -.
DR BRENDA; 4.2.3.118; 5998.
DR SABIO-RK; Q9F1Y6; -.
DR Proteomes; UP000001973; Chromosome.
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 3D-structure; Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..440
FT /note="2-methylisoborneol synthase"
FT /id="PRO_0000205354"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 46..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..67
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 197
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 349
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 353
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT HELIX 132..148
FT /evidence="ECO:0007829|PDB:3V1V"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:4LA6"
FT HELIX 163..173
FT /evidence="ECO:0007829|PDB:3V1V"
FT HELIX 180..200
FT /evidence="ECO:0007829|PDB:3V1V"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:4LA6"
FT HELIX 211..219
FT /evidence="ECO:0007829|PDB:3V1V"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:3V1V"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:3V1V"
FT HELIX 232..238
FT /evidence="ECO:0007829|PDB:3V1V"
FT HELIX 243..258
FT /evidence="ECO:0007829|PDB:3V1V"
FT HELIX 261..286
FT /evidence="ECO:0007829|PDB:3V1V"
FT HELIX 293..302
FT /evidence="ECO:0007829|PDB:3V1V"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:3V1V"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:3V1V"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:3V1V"
FT HELIX 312..316
FT /evidence="ECO:0007829|PDB:3V1V"
FT HELIX 322..325
FT /evidence="ECO:0007829|PDB:3V1V"
FT HELIX 328..348
FT /evidence="ECO:0007829|PDB:3V1V"
FT HELIX 350..353
FT /evidence="ECO:0007829|PDB:3V1V"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:3V1V"
FT HELIX 363..371
FT /evidence="ECO:0007829|PDB:3V1V"
FT HELIX 375..403
FT /evidence="ECO:0007829|PDB:3V1V"
FT HELIX 407..429
FT /evidence="ECO:0007829|PDB:3V1V"
FT TURN 431..433
FT /evidence="ECO:0007829|PDB:3V1V"
SQ SEQUENCE 440 AA; 47793 MW; 0228C9B635F4CBE2 CRC64;
MPDSGTLGTP PPEQGPTPPT TLPDVPAPVI PSASVTSAAS DFLAALHPPV TVPDPAPPPP
PAPAAGNPPD TVTGDSVLQR ILRGPTGPGT TSLAPAVRYG RQPGPEAPAS APPAAGRAVP
GLYHHPVPEP DPVRVEEVSR RIKRWAEDEV QLYPEEWEGQ FDGFSVGRYM VGCHPDAPTV
DHLMLATRLM VAENAVDDCY CEDHGGSPVG LGGRLLLAHT AIDHFHSTAE YTPTWQASLA
ADAPRRAYDS AMGYFVRAAT PSQSDRYRHD MARLHLGYLA EGAWAQTGHV PEVWEYLAMR
QFNNFRPCPT ITDTVGGYEL PADLHARPDM QRVIALAGNA TTIVNDLYSY TKELNSPGRH
LNLPVVIAER EQLCERDAYL KAVEVHNELQ HSFEAAAADL AEACPLPPVL RFLRGVAAWV
DGNHDWHRTN TYRYSLPDFW
