GPPMT_SACEN
ID GPPMT_SACEN Reviewed; 285 AA.
AC A4FG18;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Geranyl diphosphate 2-C-methyltransferase;
DE Short=GPP methyltransferase;
DE EC=2.1.1.255;
GN OrderedLocusNames=SACE_3721;
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 SAM-dependent methylation of geranyl
CC diphosphate (GPP) to yield (E)-2-methylgeranyl diphosphate (2-MeGPP).
CC {ECO:0000305|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;
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; AM420293; CAM02993.1; -; Genomic_DNA.
DR RefSeq; WP_009948569.1; NZ_PDBV01000001.1.
DR AlphaFoldDB; A4FG18; -.
DR SMR; A4FG18; -.
DR STRING; 405948.SACE_3721; -.
DR EnsemblBacteria; CAM02993; CAM02993; SACE_3721.
DR KEGG; sen:SACE_3721; -.
DR eggNOG; COG2230; Bacteria.
DR HOGENOM; CLU_1057338_0_0_11; -.
DR OMA; AHYICDI; -.
DR OrthoDB; 1518440at2; -.
DR BRENDA; 2.1.1.255; 5518.
DR Proteomes; UP000006728; Chromosome.
DR GO; GO:0008169; F:C-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; ISS: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; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Magnesium; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..285
FT /note="Geranyl diphosphate 2-C-methyltransferase"
FT /id="PRO_0000403382"
SQ SEQUENCE 285 AA; 31767 MW; 2A9AC15733CD2EA3 CRC64;
MTKSIHENGT AASVYQGSIA EYWNQEANPV NLELGEVDGY FHHHYGIGEP DWSVVEGDAA
TSHERTTREL HRLETWQAEF LLDHLGGVEP EHRIMDAGCG RGGSSFMAHE RFGCSVEGVS
LSRKQVDFAN AQARERGVAD KVAFHQLNML DTGFDTASMR AIWNNESTMY VDLHDLFAEH
SRLLARGGRY VTITGCYNDV YGLPSRAVST INAHYICDIH PRSGYFRAMA ANRLVPCAVV
DLTEATVPYW RLRAKSPLAT GIEETFIEAY TSGSFQYLLI AADRV