ID   GPPMT_STRLS             Reviewed;         300 AA.
AC   D3KYU3;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Geranyl diphosphate 2-C-methyltransferase;
DE            Short=GPP methyltransferase;
DE            EC=2.1.1.255;
GN   Name=gdpmt;
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, 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 SAM-dependent methylation of geranyl
CC       diphosphate (GPP) to yield (E)-2-methylgeranyl diphosphate (2-MeGPP).
CC       {ECO:0000269|PubMed:18492804}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate + S-adenosyl-L-methionine = (E)-2-
CC         methylgeranyl diphosphate + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:32519, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:58057, ChEBI:CHEBI:59789, ChEBI:CHEBI:61984;
CC         EC=2.1.1.255; Evidence={ECO:0000269|PubMed:18492804};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC   -!- SIMILARITY: Belongs to the geranyl diphosphate 2-C-methyltransferase
CC       family. {ECO:0000305}.
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DR   EMBL; AB547324; BAI77524.1; -; Genomic_DNA.
DR   PDB; 4F84; X-ray; 2.20 A; A=1-300.
DR   PDB; 4F85; X-ray; 2.20 A; A=1-300.
DR   PDB; 4F86; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L=1-300.
DR   PDBsum; 4F84; -.
DR   PDBsum; 4F85; -.
DR   PDBsum; 4F86; -.
DR   AlphaFoldDB; D3KYU3; -.
DR   SMR; D3KYU3; -.
DR   PRIDE; D3KYU3; -.
DR   KEGG; ag:BAI77524; -.
DR   BRENDA; 2.1.1.255; 12665.
DR   GO; GO:0008169; F:C-methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0042214; P:terpene metabolic process; IDA:UniProtKB.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Magnesium; Methyltransferase; Plasmid;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..300
FT                   /note="Geranyl diphosphate 2-C-methyltransferase"
FT                   /id="PRO_0000403380"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           28..37
FT                   /evidence="ECO:0007829|PDB:4F86"
FT   HELIX           43..50
FT                   /evidence="ECO:0007829|PDB:4F86"
FT   HELIX           66..69
FT                   /evidence="ECO:0007829|PDB:4F84"
FT   STRAND          72..74
FT                   /evidence="ECO:0007829|PDB:4F86"
FT   HELIX           77..97
FT                   /evidence="ECO:0007829|PDB:4F84"
FT   STRAND          108..113
FT                   /evidence="ECO:0007829|PDB:4F84"
FT   HELIX           118..127
FT                   /evidence="ECO:0007829|PDB:4F84"
FT   STRAND          130..136
FT                   /evidence="ECO:0007829|PDB:4F84"
FT   HELIX           138..151
FT                   /evidence="ECO:0007829|PDB:4F84"
FT   TURN            154..156
FT                   /evidence="ECO:0007829|PDB:4F84"
FT   STRAND          157..161
FT                   /evidence="ECO:0007829|PDB:4F84"
FT   STRAND          174..181
FT                   /evidence="ECO:0007829|PDB:4F84"
FT   HELIX           183..185
FT                   /evidence="ECO:0007829|PDB:4F84"
FT   HELIX           188..198
FT                   /evidence="ECO:0007829|PDB:4F84"
FT   STRAND          199..212
FT                   /evidence="ECO:0007829|PDB:4F84"
FT   HELIX           214..216
FT                   /evidence="ECO:0007829|PDB:4F84"
FT   HELIX           221..230
FT                   /evidence="ECO:0007829|PDB:4F84"
FT   HELIX           237..246
FT                   /evidence="ECO:0007829|PDB:4F84"
FT   STRAND          249..256
FT                   /evidence="ECO:0007829|PDB:4F84"
FT   HELIX           258..268
FT                   /evidence="ECO:0007829|PDB:4F84"
FT   STRAND          271..273
FT                   /evidence="ECO:0007829|PDB:4F84"
FT   HELIX           278..287
FT                   /evidence="ECO:0007829|PDB:4F84"
FT   STRAND          288..299
FT                   /evidence="ECO:0007829|PDB:4F84"
SQ   SEQUENCE   300 AA;  32881 MW;  6605485E66D19B00 CRC64;
     MAAASAPVPG PGGASSTARG RIPAPATPYQ EDIARYWNNE ARPVNLRLGD VDGLYHHHYG
     IGAVDHAALG DPGDGGYEAR LIAELHRLES AQAEFLLDHL GPVGPGDTLV DAGCGRGGSM
     VMAHQRFGCK VEGVTLSAAQ AEFGNRRARE LGIDDHVRSR VCNMLDTPFE KGTVAASWNN
     ESSMYVDLHD VFAEHSRFLR VGGRYVTVTG CWNPRYGQPS KWVSQINAHF ECNIHSRREY
     LRAMADNRLV PQTVVDLTPE TLPYWELRAT SSLVTGIEEA FIESYRDGSF QYVLIAADRV