ID   BOMT_BOTBR              Reviewed;         379 AA.
AC   H2E7T7;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   03-AUG-2022, entry version 31.
DE   RecName: Full=Botryococcene C-methyltransferase;
DE            EC=2.1.1.263 {ECO:0000269|PubMed:22241476};
DE   AltName: Full=Triterpene methyltransferase 3;
GN   Name=TMT-3;
OS   Botryococcus braunii (Green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Trebouxiophyceae incertae sedis; Elliptochloris clade; Botryococcus.
OX   NCBI_TaxID=38881;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=22241476; DOI=10.1074/jbc.m111.316059;
RA   Niehaus T.D., Kinison S., Okada S., Yeo Y.S., Bell S.A., Cui P.,
RA   Devarenne T.P., Chappell J.;
RT   "Functional identification of triterpene methyltransferases from
RT   Botryococcus braunii race B.";
RL   J. Biol. Chem. 287:8163-8173(2012).
CC   -!- FUNCTION: Converts botryococcene to mono- and dimethyl derivatives, but
CC       not to tri- and tetramethylated products. Unable to methylate
CC       cycloartenol, zymosterol or lanosterol, but can also use squalene as
CC       substrate. Methylates both C-3 and C22 positions, but only C-3 position
CC       in monomethylated squalenes. In contrast, monomethylated botryococcene
CC       occured mainly at the C-20 position yielding showacene, but also at the
CC       C-3 position yielding isoshowacene. {ECO:0000269|PubMed:22241476}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=C30 botryococcene + 2 S-adenosyl-L-methionine = 3,20-dimethyl-
CC         1,2,21,22-tetradehydro-2,3,20,21-tetrahydrobotryococcene + 2 H(+) + 2
CC         S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:34655, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:70786,
CC         ChEBI:CHEBI:70865; EC=2.1.1.263;
CC         Evidence={ECO:0000269|PubMed:22241476};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=68.9 uM for botryococcene {ECO:0000269|PubMed:22241476};
CC   -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000305}; Single-pass
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Erg6/SMT family. {ECO:0000255|PROSITE-ProRule:PRU01022}.
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DR   EMBL; JN828964; AEY68258.1; -; mRNA.
DR   AlphaFoldDB; H2E7T7; -.
DR   SMR; H2E7T7; -.
DR   KEGG; ag:AEY68258; -.
DR   BioCyc; MetaCyc:MON-17325; -.
DR   SABIO-RK; H2E7T7; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006694; P:steroid biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR013216; Methyltransf_11.
DR   InterPro; IPR030384; MeTrfase_SMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR013705; Sterol_MeTrfase_C.
DR   Pfam; PF08241; Methyltransf_11; 1.
DR   Pfam; PF08498; Sterol_MT_C; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51685; SAM_MT_ERG6_SMT; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Methyltransferase; Microsome; S-adenosyl-L-methionine; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..379
FT                   /note="Botryococcene C-methyltransferase"
FT                   /id="PRO_0000421357"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   379 AA;  41783 MW;  DA587B5ED164F3CB CRC64;
     MALDLLSSYA PGLVESLLTW KGAAGLAAAV ALGYIIISNL PGRQVAKPSL LQVRTGGVAF
     EKVAEVVADY SDSYGQTEKG ELIVKDNNKI VSLANTFYDL ITDGYEWGWG SGFHFSHRLP
     GMSFNASQLL HESRMASFLR LKPGMQVLDV GCGVGNPGRT VAACSGAVVT GITINAYQIK
     RAELHTKRAG LVGYFKPVQG NFCAMPFQDK SFDAAFAMDS TCHAPKLEDV YSEVFRVLKP
     GAYFATYEWV STKNYDSNNP EHVKCMNSII LGNGLPNIRS WKQAEEAGKN VGFNLLTSLD
     MATNSPIGKP WYSVPERMVN WGLFRFHKAC IRTASTLHLL PPESWKFFYI LAEMAENLVK
     GGQWDIFTPM HLLIFQKPE