GPPMT_STRCO
ID GPPMT_STRCO Reviewed; 292 AA.
AC Q9F1Y5;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Geranyl diphosphate 2-C-methyltransferase;
DE Short=GPP methyltransferase;
DE EC=2.1.1.255;
GN OrderedLocusNames=SCO7701; ORFNames=orf4, SCBAC12C8.02;
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.;
RT "S.coelicolor orf3 orf1 p52 orf2 orf4 orf5.";
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 PARAMETERS, 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 SAM-dependent methylation of geranyl
CC diphosphate (GPP) to yield (E)-2-methylgeranyl diphosphate (2-MeGPP).
CC {ECO:0000269|PubMed:18563898}.
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:18563898};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:18563898};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13.1 uM for geranyl diphosphate {ECO:0000269|PubMed:18563898};
CC KM=4.3 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:18563898};
CC -!- SIMILARITY: Belongs to the geranyl diphosphate 2-C-methyltransferase
CC family. {ECO:0000305}.
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DR EMBL; AB035202; BAB20434.1; -; Genomic_DNA.
DR EMBL; AL939132; CAC44557.1; -; Genomic_DNA.
DR RefSeq; NP_631739.1; NC_003888.3.
DR RefSeq; WP_011031840.1; NZ_VNID01000005.1.
DR PDB; 3VC1; X-ray; 1.82 A; A/B/C/D/E/F/G/H/I/J/K/L=1-292.
DR PDB; 3VC2; X-ray; 2.05 A; A/B/C/D/E/F/G/H/I/J/K/L=1-292.
DR PDBsum; 3VC1; -.
DR PDBsum; 3VC2; -.
DR AlphaFoldDB; Q9F1Y5; -.
DR SMR; Q9F1Y5; -.
DR STRING; 100226.SCO7701; -.
DR GeneID; 1103139; -.
DR KEGG; sco:SCO7701; -.
DR PATRIC; fig|100226.15.peg.7821; -.
DR eggNOG; COG2230; Bacteria.
DR HOGENOM; CLU_1057338_0_0_11; -.
DR InParanoid; Q9F1Y5; -.
DR OMA; AHFECNI; -.
DR PhylomeDB; Q9F1Y5; -.
DR BioCyc; MetaCyc:MON-17559; -.
DR BRENDA; 2.1.1.255; 5998.
DR SABIO-RK; Q9F1Y5; -.
DR Proteomes; UP000001973; Chromosome.
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; IPR013216; Methyltransf_11.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF08241; Methyltransf_11; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Magnesium; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..292
FT /note="Geranyl diphosphate 2-C-methyltransferase"
FT /id="PRO_0000403379"
FT HELIX 7..12
FT /evidence="ECO:0007829|PDB:3VC1"
FT HELIX 20..31
FT /evidence="ECO:0007829|PDB:3VC1"
FT HELIX 35..41
FT /evidence="ECO:0007829|PDB:3VC1"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:3VC1"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:3VC1"
FT HELIX 69..89
FT /evidence="ECO:0007829|PDB:3VC1"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:3VC1"
FT HELIX 110..119
FT /evidence="ECO:0007829|PDB:3VC1"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:3VC1"
FT HELIX 130..142
FT /evidence="ECO:0007829|PDB:3VC1"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:3VC1"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:3VC1"
FT STRAND 166..173
FT /evidence="ECO:0007829|PDB:3VC1"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:3VC1"
FT HELIX 180..190
FT /evidence="ECO:0007829|PDB:3VC1"
FT STRAND 191..204
FT /evidence="ECO:0007829|PDB:3VC1"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:3VC1"
FT HELIX 213..222
FT /evidence="ECO:0007829|PDB:3VC1"
FT HELIX 229..237
FT /evidence="ECO:0007829|PDB:3VC1"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:3VC1"
FT STRAND 241..248
FT /evidence="ECO:0007829|PDB:3VC1"
FT HELIX 250..260
FT /evidence="ECO:0007829|PDB:3VC1"
FT HELIX 270..278
FT /evidence="ECO:0007829|PDB:3VC1"
FT STRAND 281..291
FT /evidence="ECO:0007829|PDB:3VC1"
SQ SEQUENCE 292 AA; 32824 MW; 73D2386F9D40A48D CRC64;
MTTETTTATA TAKIPAPATP YQEDIARYWN NEARPVNLRL GDVDGLYHHH YGIGPVDRAA
LGDPEHSEYE KKVIAELHRL ESAQAEFLMD HLGQAGPDDT LVDAGCGRGG SMVMAHRRFG
SRVEGVTLSA AQADFGNRRA RELRIDDHVR SRVCNMLDTP FDKGAVTASW NNESTMYVDL
HDLFSEHSRF LKVGGRYVTI TGCWNPRYGQ PSKWVSQINA HFECNIHSRR EYLRAMADNR
LVPHTIVDLT PDTLPYWELR ATSSLVTGIE KAFIESYRDG SFQYVLIAAD RV
