SDMT_PARMW
ID SDMT_PARMW Reviewed; 280 AA.
AC Q7U4Z9;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Dimethylglycine N-methyltransferase;
DE EC=2.1.1.161;
GN Name=bsmB; Synonyms=sdmt; OrderedLocusNames=SYNW1913;
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 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 dimethylglycine to betaine with
CC S-adenosylmethionine (AdoMet) acting as the methyl donor. It has strict
CC specificity for dimethylglycine as the methyl group acceptors.
CC {ECO:0000269|PubMed:17019606}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N,N-dimethylglycine + S-adenosyl-L-methionine = glycine
CC betaine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:10072,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17750, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:58251, ChEBI:CHEBI:59789; EC=2.1.1.161;
CC Evidence={ECO:0000269|PubMed:17019606};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.11 mM for dimethylglycine (at pH 8.5 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:17019606};
CC KM=0.41 mM for AdoMet (at pH 8.5 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:17019606};
CC Vmax=1.06 umol/min/mg enzyme with AdoMet as substrate (at pH 8.5 and
CC at 37 degrees Celsius) {ECO:0000269|PubMed:17019606};
CC Vmax=1.18 umol/min/mg enzyme with dimethylglycine as substrate (at pH
CC 8.5 and at 37 degrees) {ECO:0000269|PubMed:17019606};
CC pH dependence:
CC Optimum pH is around 8.5 for dimethylglycine.
CC {ECO:0000269|PubMed:17019606};
CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC glycine pathway; betaine from glycine: step 3/3.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17019606}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
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DR EMBL; BX569694; CAE08428.1; -; Genomic_DNA.
DR RefSeq; WP_011128771.1; NC_005070.1.
DR AlphaFoldDB; Q7U4Z9; -.
DR SMR; Q7U4Z9; -.
DR STRING; 84588.SYNW1913; -.
DR EnsemblBacteria; CAE08428; CAE08428; SYNW1913.
DR KEGG; syw:SYNW1913; -.
DR eggNOG; COG2230; Bacteria.
DR HOGENOM; CLU_039068_6_2_3; -.
DR OMA; MDAGLGH; -.
DR OrthoDB; 1518440at2; -.
DR BRENDA; 2.1.1.161; 9130.
DR UniPathway; UPA00530; UER00383.
DR Proteomes; UP000001422; Chromosome.
DR GO; GO:0052729; F:dimethylglycine N-methyltransferase activity; IDA:UniProtKB.
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; 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..280
FT /note="Dimethylglycine N-methyltransferase"
FT /id="PRO_0000413615"
SQ SEQUENCE 280 AA; 30752 MW; 711CFCD662447E74 CRC64;
MGTTNGCAAD SVAATYYDSQ DADQFYEQVW GGEDIHIGLY ATPDEAIATA SDRTVHALLD
LADPLPQGGC VVDLGAGYGG ASRRLARWSE RPVHAINISA VENDRHRRLN VDAGLEQQIT
VHDASFEQVP MADASADLVW SQDAILHAGD RAKVLAEVSR LLKPGGCFVF TDPMAADGVE
MGLLQPILDR IHLPDLASPS RYKAWGEAVG LTMEVWDERT EMLVRHYDRV RQDTRLRRAE
LETSISSGYL DRMDVGLGHW VDGGQQGRLS WGLMRLRKPG