GSDMT_ACTHA
ID GSDMT_ACTHA Reviewed; 565 AA.
AC Q9KJ20;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Glycine/sarcosine/dimethylglycine N-methyltransferase;
DE EC=2.1.1.156 {ECO:0000269|PubMed:10896953};
DE EC=2.1.1.157 {ECO:0000269|PubMed:10896953};
DE AltName: Full=Dimethylglycine N-methyltransferase;
OS Actinopolyspora halophila.
OC Bacteria; Actinobacteria; Actinopolysporales; Actinopolysporaceae;
OC Actinopolyspora.
OX NCBI_TaxID=1850;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A METHYLTRANSFERASE,
RP FUNCTION IN BETAINE BIOSYNTHESIS, CATALYTIC ACTIVITY, AND SUBUNIT.
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).
CC -!- FUNCTION: Catalyzes the methylation of glycine, sarcosine and
CC dimethylglycine to sarcosine, dimethylglycine and betaine,
CC respectively, with S-adenosylmethionine (AdoMet) acting as the methyl
CC donor. {ECO:0000269|PubMed:10896953}.
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:10896953};
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};
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 -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC glycine pathway; betaine from glycine: step 3/3.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10896953}.
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; AF216283; AAF87204.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9KJ20; -.
DR SMR; Q9KJ20; -.
DR KEGG; ag:AAF87204; -.
DR BioCyc; MetaCyc:MON-8544; -.
DR BRENDA; 2.1.1.156; 7834.
DR UniPathway; UPA00530; UER00381.
DR UniPathway; UPA00530; UER00382.
DR UniPathway; UPA00530; UER00383.
DR GO; GO:0052729; F:dimethylglycine N-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0017174; F:glycine N-methyltransferase activity; IEA:UniProtKB-EC.
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; -; 2.
DR InterPro; IPR014369; Gly/Sar_N_MeTrfase.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF08241; Methyltransf_11; 1.
DR Pfam; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF53335; SSF53335; 2.
DR PROSITE; PS51600; SAM_GNMT; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..565
FT /note="Glycine/sarcosine/dimethylglycine N-
FT methyltransferase"
FT /id="PRO_0000413613"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 45
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT BINDING 53
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT BINDING 62
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT BINDING 86
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT BINDING 107
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT BINDING 134..135
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT BINDING 152
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00932"
SQ SEQUENCE 565 AA; 64719 MW; 856F862BC68A149C CRC64;
MTKSVDDLAR GDQAGDEQDP VHREQQTFGD NPLEVRDTDH YMHEYVGGFV DKWDDLIDWK
KRYESEGSFF IDQLRARGVE TVLDAAAGTG FHSVRLLEEG FETVSADGSP QMLAKAFSNG
LAYNGHILRV VNADWRWLNR DVHGEYDAII CLGNSFTHLF SERDRRKTLA EFYAMLKHDG
VLIIDQRNYD SILDTGFSSK HTYYYAGEDV SAEPDHIDDG LARFKYTFPD KSEFFLNMYP
LRKDYMRRLM REVGFQRIDT YGDFQETYGE DEPDFYIHVA EKSYRTEDEF VDMYSNAVHT
ARDYYNSEDA DNFYYHVWGG NDIHVGLYQT PQEDIATASE RTVQRMAGKV DISPETRILD
LGAGYGGAAR YLARTYGCHV TCLNLSEVEN QRNREITRAE GLEHLIEVTD GSFEDLPYQD
NAFDVVWSQD SFLHSGDRSR VMEEVTRVLK PKGSVLFTDP MASDSAKKNE LGPILDRLHL
DSLGSPGFYR KELTRLGLQN IEFEDLSEYL PVHYGRVLEV LESRENELAG FIGEEYRAHM
KTGLRNWVQA GNGGSLAWGI IHARA
