ID   SDMT_HALHR              Reviewed;         279 AA.
AC   Q9KJ21;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Sarcosine/dimethylglycine N-methyltransferase;
DE            EC=2.1.1.157;
OS   Halorhodospira halochloris (Ectothiorhodospira halochloris).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Halorhodospira.
OX   NCBI_TaxID=1052;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN BETAINE BIOSYNTHESIS, AND
RP   CATALYTIC ACTIVITY.
RX   PubMed=10896953; DOI=10.1074/jbc.m910111199;
RA   Nyyssola A., Kerovuo J., Kaukinen P., von Weymarn N., Reinikainen T.;
RT   "Extreme halophiles synthesize betaine from glycine by methylation.";
RL   J. Biol. Chem. 275:22196-22201(2000).
RN   [2]
RP   FUNCTION AS A METHYLTRANSFERASE AND IN BETAINE BIOSYNTHESIS, CATALYTIC
RP   ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBUNIT.
RX   PubMed=11319079; DOI=10.1128/aem.67.5.2044-2050.2001;
RA   Nyyssola A., Reinikainen T., Leisola M.;
RT   "Characterization of glycine sarcosine N-methyltransferase and sarcosine
RT   dimethylglycine N-methyltransferase.";
RL   Appl. Environ. Microbiol. 67:2044-2050(2001).
CC   -!- FUNCTION: Catalyzes the methylation of sarcosine and dimethylglycine to
CC       dimethylglycine and betaine, respectively, with S-adenosylmethionine
CC       (AdoMet) acting as the methyl donor. It has strict specificity for
CC       sarcosine and dimethylglycine as the methyl group acceptors.
CC       {ECO:0000269|PubMed:10896953, ECO:0000269|PubMed:11319079}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 S-adenosyl-L-methionine + sarcosine = glycine betaine + 2
CC         H(+) + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:32467,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17750, ChEBI:CHEBI:57433,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.157;
CC         Evidence={ECO:0000269|PubMed:10896953, ECO:0000269|PubMed:11319079};
CC   -!- ACTIVITY REGULATION: p-chloromercuribenzoate acid inhibits 23% of the
CC       SDMT activities on sarcosine and dimethylglycine, and S-
CC       adenosylhomocysteine (AdoHcy) inhibits completely GSMT activities.
CC       {ECO:0000269|PubMed:11319079}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.16 mM for AdoMet (with dimethylglycine at pH 7.4 and at 37
CC         degrees Celsius) {ECO:0000269|PubMed:11319079};
CC         KM=0.21 mM for AdoMet (with sarcosine at pH 7.4 and at 37 degrees
CC         Celsius) {ECO:0000269|PubMed:11319079};
CC         KM=4.9 mM for dimethylglycine (at pH 7.4 and at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:11319079};
CC         KM=6.1 mM for sarcosine (at pH 7.4 and at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:11319079};
CC         Vmax=1.1 umol/min/mg enzyme with AdoMet as substrate (with sarcosine
CC         at pH 7.4 and at 37 degrees Celsius) {ECO:0000269|PubMed:11319079};
CC         Vmax=1.3 umol/min/mg enzyme with sarcosine as substrate (at pH 7.4
CC         and at 37 degrees) {ECO:0000269|PubMed:11319079};
CC         Vmax=6.1 umol/min/mg enzyme with AdoMet as substrate (with
CC         dimethylglycine at pH 7.4 and at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:11319079};
CC         Vmax=7.4 umol/min/mg enzyme with dimethylglycine as substrate (at pH
CC         7.4 and at 37 degrees Celsius) {ECO:0000269|PubMed:11319079};
CC       pH dependence:
CC         Optimum pH is around 8 and 7.6 for sarcosine and dimethylglycine,
CC         respectively. The pH optimum appears to depend on the buffer used.
CC         {ECO:0000269|PubMed:11319079};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC       glycine pathway; betaine from glycine: step 2/3.
CC   -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC       glycine pathway; betaine from glycine: step 3/3.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11319079}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF216282; AAF87203.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9KJ21; -.
DR   SMR; Q9KJ21; -.
DR   KEGG; ag:AAF87203; -.
DR   BioCyc; MetaCyc:MON-8543; -.
DR   BRENDA; 2.1.1.157; 2037.
DR   UniPathway; UPA00530; UER00382.
DR   UniPathway; UPA00530; UER00383.
DR   GO; GO:0052729; F:dimethylglycine N-methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0052730; F:sarcosine N-methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0019286; P:glycine betaine biosynthetic process from glycine; IDA:UniProtKB.
DR   GO; GO:0032259; P:methylation; 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   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..279
FT                   /note="Sarcosine/dimethylglycine N-methyltransferase"
FT                   /id="PRO_0000413614"
SQ   SEQUENCE   279 AA;  32228 MW;  579337A6915E66D5 CRC64;
     MATRYDDQAI ETARQYYNSE DADNFYAIIW GGEDIHIGLY NDDEEPIADA SRRTVERMSS
     LSRQLGPDSY VLDMGAGYGG SARYLAHKYG CKVAALNLSE RENERDRQMN KEQGVDHLIE
     VVDAAFEDVP YDDGVFDLVW SQDSFLHSPD RERVLREASR VLRSGGEFIF TDPMQADDCP
     EGVIQPILDR IHLETMGTPN FYRQTLRDLG FEEITFEDHT HQLPRHYGRV RRELDRREGE
     LQGHVSAEYI ERMKNGLDHW VNGGNKGYLT WGIFYFRKG