GSMT_PARMW
ID GSMT_PARMW Reviewed; 282 AA.
AC Q7U4Z8;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Glycine/sarcosine N-methyltransferase;
DE EC=2.1.1.156 {ECO:0000269|PubMed:17019606};
GN Name=bsmA; Synonyms=gsmt; OrderedLocusNames=SYNW1914;
OS Parasynechococcus marenigrum (strain WH8102).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Parasynechococcus; Parasynechococcus marenigrum.
OX NCBI_TaxID=84588;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH8102;
RX PubMed=12917641; DOI=10.1038/nature01943;
RA Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT "The genome of a motile marine Synechococcus.";
RL Nature 424:1037-1042(2003).
RN [2]
RP FUNCTION IN THE BETAINE BIOSYNTHESIS, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND NOMENCLATURE.
RX PubMed=17019606; DOI=10.1007/s00203-006-0167-8;
RA Lu W.D., Chi Z.M., Su C.D.;
RT "Identification of glycine betaine as compatible solute in Synechococcus
RT sp. WH8102 and characterization of its N-methyltransferase genes involved
RT in betaine synthesis.";
RL Arch. Microbiol. 186:495-506(2006).
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:17019606}.
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:17019606};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.30 mM for AdoMet (with glycine at pH 8.2 and at 37 degrees
CC Celsius) {ECO:0000269|PubMed:17019606};
CC KM=0.44 mM for AdoMet (with sarcosine at pH 8.0 and at 37 degrees
CC Celsius) {ECO:0000269|PubMed:17019606};
CC KM=2.94 mM for sarcosine (at pH 8.0 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:17019606};
CC KM=5.22 mM for glycine (at pH 8.2 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:17019606};
CC Vmax=0.74 umol/min/mg enzyme with AdoMet as substrate (with sarcosine
CC at pH 8.0 and at 37 degrees Celsius) {ECO:0000269|PubMed:17019606};
CC Vmax=0.78 umol/min/mg enzyme with sarcosine as substrate (at pH 8.0
CC and at 37 degrees Celsius) {ECO:0000269|PubMed:17019606};
CC Vmax=1.30 umol/min/mg enzyme with AdoMet as substrate (with glycine
CC at pH 8.2 and at 37 degrees Celsius) {ECO:0000269|PubMed:17019606};
CC Vmax=1.48 umol/min/mg enzyme with glycine as substrate (at pH 8.2 and
CC at 37 degrees Celsius) {ECO:0000269|PubMed:17019606};
CC pH dependence:
CC Optimum pH is around 8.2 and 8.0 for glycine and sarcosine,
CC respectively. {ECO:0000269|PubMed:17019606};
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:17019606}.
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; BX569694; CAE08429.1; -; Genomic_DNA.
DR RefSeq; WP_011128772.1; NC_005070.1.
DR AlphaFoldDB; Q7U4Z8; -.
DR SMR; Q7U4Z8; -.
DR STRING; 84588.SYNW1914; -.
DR EnsemblBacteria; CAE08429; CAE08429; SYNW1914.
DR KEGG; syw:SYNW1914; -.
DR eggNOG; COG2226; Bacteria.
DR HOGENOM; CLU_069129_0_0_3; -.
DR OMA; DHYQQEY; -.
DR OrthoDB; 1518440at2; -.
DR BRENDA; 2.1.1.156; 9130.
DR UniPathway; UPA00530; UER00381.
DR UniPathway; UPA00530; UER00382.
DR Proteomes; UP000001422; Chromosome.
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 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..282
FT /note="Glycine/sarcosine N-methyltransferase"
FT /id="PRO_0000413612"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 35
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 52
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT BINDING 76
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT BINDING 97
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT BINDING 123..124
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT BINDING 141
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
SQ SEQUENCE 282 AA; 32894 MW; 0A3235C5445874DC CRC64;
MTSTQNHPLQ TQDDQQRFGQ SPESVRETDH YQQEYIEDFT DRWDRLIDWN ARAEAEGDFF
IRLLKEHGAR SVLDVATGTG FHSIRLLEEG FDVVSADGSP NMLARAFRNA RNRDQLLRTS
QADWRFLNRD IHGEFDAVIC LGNSFTHLFK ERDRRKALAE YYAVLKHNGI LILDHRNYDR
LLEGGSAVRQ GKGNVYCGKD VEVGPEHVDE GLARFRYSFS DGGVYHLNMF PLRYGYVRRL
MSEVGFQQIT SFGDYQRDFE NPDFYVHVAE KEYRFDVDTT MH
