ID   GSMT_HALHR              Reviewed;         268 AA.
AC   Q9KJ22;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Glycine/sarcosine N-methyltransferase;
DE            EC=2.1.1.156 {ECO:0000269|PubMed:11319079};
OS   Halorhodospira halochloris (Ectothiorhodospira halochloris).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Halorhodospira.
OX   NCBI_TaxID=1052;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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, FUNCTION IN THE BETAINE BIOSYNTHESIS,
RP   CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL 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 glycine and sarcosine to
CC       sarcosine and dimethylglycine, respectively, with S-adenosylmethionine
CC       (AdoMet) acting as the methyl donor. It has strict specificity for
CC       glycine and sarcosine as the methyl group acceptors.
CC       {ECO:0000269|PubMed:11319079}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycine + 2 S-adenosyl-L-methionine = 2 H(+) + N,N-
CC         dimethylglycine + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:32463,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57305, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:58251, ChEBI:CHEBI:59789; EC=2.1.1.156;
CC         Evidence={ECO:0000269|PubMed:11319079};
CC   -!- ACTIVITY REGULATION: p-chloromercuribenzoic acid inhibits more than 95%
CC       of the GSMT activities on glycine and sarcosine, and S-
CC       adenosylhomocysteine (AdoHcy) inhibits completely GSMT activities.
CC       {ECO:0000269|PubMed:11319079}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.3 mM for sarcosine (at pH 7.4 and at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:11319079};
CC         KM=18 mM for glycine (at pH 7.4 and at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:11319079};
CC         KM=0.28 mM for AdoMet (with sarcosine at pH 7.4 and at 37 degrees
CC         Celsius) {ECO:0000269|PubMed:11319079};
CC         KM=0.42 mM for AdoMet (with glycine at pH 7.4 and at 37 degrees
CC         Celsius) {ECO:0000269|PubMed:11319079};
CC         Vmax=0.12 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=0.15 umol/min/mg enzyme with sarcosine as substrate (at pH 7.4
CC         and at 37 degrees) {ECO:0000269|PubMed:11319079};
CC         Vmax=1.0 umol/min/mg enzyme with AdoMet as substrate (with glycine at
CC         pH 7.4 and at 37 degrees Celsius) {ECO:0000269|PubMed:11319079};
CC         Vmax=1.1 umol/min/mg enzyme with glycine as substrate (at pH 7.4 and
CC         at 37 degrees) {ECO:0000269|PubMed:11319079};
CC       pH dependence:
CC         Optimum pH is around 7.4 and 7.9 for glycine and sarcosine,
CC         respectively. {ECO:0000269|PubMed:11319079};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC       glycine pathway; betaine from glycine: step 1/3.
CC   -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC       glycine pathway; betaine from glycine: step 2/3.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11319079}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Glycine N-methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00932}.
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DR   EMBL; AF216281; AAF87202.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9KJ22; -.
DR   SMR; Q9KJ22; -.
DR   KEGG; ag:AAF87202; -.
DR   BioCyc; MetaCyc:MON-8542; -.
DR   BRENDA; 2.1.1.156; 2037.
DR   UniPathway; UPA00530; UER00381.
DR   UniPathway; UPA00530; UER00382.
DR   GO; GO:0017174; F:glycine N-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052730; F:sarcosine N-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019286; P:glycine betaine biosynthetic process from glycine; IDA:UniProtKB.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR014369; Gly/Sar_N_MeTrfase.
DR   InterPro; IPR041698; Methyltransf_25.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR16458; PTHR16458; 1.
DR   Pfam; PF13649; Methyltransf_25; 1.
DR   PIRSF; PIRSF000385; Gly_N-mtase; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51600; SAM_GNMT; 1.
PE   1: Evidence at protein level;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..268
FT                   /note="Glycine/sarcosine N-methyltransferase"
FT                   /id="PRO_0000413611"
FT   BINDING         26
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT   BINDING         34
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT   BINDING         43
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT   BINDING         67
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT   BINDING         88
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT   BINDING         114..115
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT   BINDING         132
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT   BINDING         134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT   BINDING         167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT   BINDING         206
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
SQ   SEQUENCE   268 AA;  31184 MW;  6FEF20EB9DA52186 CRC64;
     MNTTTEQDFG ADPTKVRDTD HYTEEYVDGF VDKWDDLIDW DSRAKSEGDF FIQELKKRGA
     TRILDAATGT GFHSVRLLEA GFDVVSADGS AEMLAKAFEN GRKRGHILRT VQVDWRWLNR
     DIHGRYDAII CLGNSFTHLF NEKDRRKTLA EFYSALNPEG VLILDQRNYD GILDHGYDSS
     HSYYYCGEGV SVYPEHVDDG LARFKYEFND GSTYFLNMFP LRKDYTRRLM HEVGFQKIDT
     YGDFKATYRD ADPDFFIHVA EKEYREED