ID GSMT_APHHA Reviewed; 265 AA.
AC Q83WC4;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 13-SEP-2023, entry version 79.
DE RecName: Full=Glycine/sarcosine N-methyltransferase {ECO:0000305};
DE EC=2.1.1.156 {ECO:0000269|PubMed:12466265};
DE AltName: Full=ApGSMT {ECO:0000303|PubMed:12466265};
OS Aphanothece halophytica.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Aphanothece.
OX NCBI_TaxID=72020;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A METHYLTRANSFERASE AND IN
RP BETAINE BIOSYNTHESIS, CATALYTIC ACTIVITY, PATHWAY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT, AND
RP MUTAGENESIS OF ARG-169.
RX PubMed=12466265; DOI=10.1074/jbc.m210970200;
RA Waditee R., Tanaka Y., Aoki K., Hibino T., Jikuya H., Takano J., Takabe T.,
RA Takabe T.;
RT "Isolation and functional characterization of N-methyltransferases that
RT catalyze betaine synthesis from glycine in a halotolerant photosynthetic
RT organism Aphanothece halophytica.";
RL J. Biol. Chem. 278:4932-4942(2003).
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. {ECO:0000269|PubMed:12466265}.
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:12466265};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32464;
CC Evidence={ECO:0000269|PubMed:12466265};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-
CC homocysteine + sarcosine; Xref=Rhea:RHEA:19937, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57433, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789; Evidence={ECO:0000269|PubMed:12466265};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19938;
CC Evidence={ECO:0000269|PubMed:12466265};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + sarcosine = H(+) + N,N-
CC dimethylglycine + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:15453,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57433, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:58251, ChEBI:CHEBI:59789;
CC Evidence={ECO:0000269|PubMed:12466265};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15454;
CC Evidence={ECO:0000269|PubMed:12466265};
CC -!- ACTIVITY REGULATION: Inhibited by acetate, dimethylglycine and S-
CC adenosyl-L-homocysteine. {ECO:0000269|PubMed:12466265}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.6 mM for S-adenosyl-L-homocysteine (at pH 8.8 and at 37 degrees
CC Celsius) {ECO:0000269|PubMed:12466265};
CC KM=0.8 mM for sarcosine (at pH 8.8 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:12466265};
CC KM=1.5 mM for glycine (at pH 8.8 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:12466265};
CC Vmax=0.50 umol/min/mg enzyme (at pH 8.8 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:12466265};
CC pH dependence:
CC Optimum pH is 8.8. The activities remain high at more alkaline pH but
CC decrease sharply at the acidic side of the optimal pH.
CC {ECO:0000269|PubMed:12466265};
CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC glycine pathway; betaine from glycine: step 1/3.
CC {ECO:0000269|PubMed:12466265}.
CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC glycine pathway; betaine from glycine: step 2/3.
CC {ECO:0000269|PubMed:12466265}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12466265}.
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; AB094497; BAC56939.1; -; Genomic_DNA.
DR AlphaFoldDB; Q83WC4; -.
DR SMR; Q83WC4; -.
DR KEGG; ag:BAC56939; -.
DR BioCyc; MetaCyc:MONOMER-8562; -.
DR BRENDA; 2.1.1.156; 383.
DR UniPathway; UPA00530; UER00381.
DR UniPathway; UPA00530; UER00382.
DR GO; GO:0017174; F:glycine 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 CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.30.46.10; Glycine N-methyltransferase, chain A, domain 1; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR014369; Gly/Sar_N_MeTrfase.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR16458; GLYCINE N-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR16458:SF2; GLYCINE N-METHYLTRANSFERASE; 1.
DR Pfam; PF13649; Methyltransf_25; 1.
DR PIRSF; PIRSF000385; Gly_N-mtase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51600; SAM_GNMT; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..265
FT /note="Glycine/sarcosine N-methyltransferase"
FT /id="PRO_0000412534"
FT BINDING 28
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT BINDING 36
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT BINDING 45
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT BINDING 69
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT BINDING 90
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT BINDING 116..117
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT BINDING 134
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT MUTAGEN 169
FT /note="R->E: Completely inactive."
FT /evidence="ECO:0000269|PubMed:12466265"
FT MUTAGEN 169
FT /note="R->K: The affinity for glycine and sarcosine
FT decrease 50- and 63-fold, respectively, whereas the
FT affinity for AdoMet changes only within 2-fold. Not able to
FT catalyze the methylation of dimethylglycine."
FT /evidence="ECO:0000269|PubMed:12466265"
SQ SEQUENCE 265 AA; 31213 MW; DD65C73F70E44536 CRC64;
MAIKEKQVQD YGENPIEVRD SDHYQNEYIE GFVEKWDELI NWHARSSSEG EFFIKTLKEH
GAKRVLDAAT GTGFHSIRLI EAGFDVASVD GSVEMLVKAF ENATRKDQIL RTVHSDWRQV
TRHIQERFDA VICLGNSFTH LFSEEDRRKT LAEFYSVLKH DGILILDQRN YDLILDEGFK
SKHTYYYCGD NVKAEPEYVD DGLARFRYEF PDQSVYHLNM FPLRKDYVRR LLHEVGFQDI
TTYGDFQETY HQDDPDFYIH VAKKD
//
