EzCatDB: D00075
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DB codeD00075
CATH domainDomain 13.30.46.10 : Glycine N-methyltransferase; chain A, domain 1Catalytic domain
Domain 23.40.50.150 : Rossmann foldCatalytic domain
E.C.2.1.1.20
CSA1xva
MACiEM0023

CATH domainRelated DB codes (homologues)
3.40.50.150 : Rossmann foldS00637,S00639,S00262,S00261,S00291,S00412,D00076,D00079,D00080,D00082,D00083,D00823

Enzyme Name
UniProtKBKEGG

P13255
Protein nameGlycine N-methyltransferaseglycine N-methyltransferase
glycine methyltransferase
S-adenosyl-L-methionine:glycine methyltransferase
GNMT
SynonymsEC 2.1.1.20
Folate-binding protein
RefSeqNP_058780.1 (Protein)
NM_017084.1 (DNA/RNA sequence)

KEGG pathways
MAP codePathways
MAP00260Glycine, serine and threonine metabolism

UniProtKB:Accession NumberP13255
Entry nameGNMT_RAT
ActivityS-adenosyl-L-methionine + glycine = S- adenosyl-L-homocysteine + sarcosine.
SubunitHomotetramer.
Subcellular locationCytoplasm.
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00019C00037C00021C00213
CompoundS-Adenosyl-L-methionineGlycineS-Adenosyl-L-homocysteineSarcosine
Typeamino acids,amine group,nucleoside,sulfonium ionamino acidsamino acids,amine group,nucleoside,sulfide groupamino acids
ChEBI67040
15428
57305
16680
57856
15611
57433
PubChem34755
750
5257127
439155
25246222
7311726
1088
            
1bhjA01UnboundUnboundUnboundUnbound
1bhjB01UnboundUnboundUnboundUnbound
1d2cA01UnboundUnboundUnboundUnbound
1d2cB01UnboundUnboundUnboundUnbound
1d2gA01UnboundUnboundUnboundUnbound
1d2gB01UnboundUnboundUnboundUnbound
1d2hA01UnboundUnboundUnboundUnbound
1d2hB01UnboundUnboundUnboundUnbound
1d2hC01UnboundUnboundUnboundUnbound
1d2hD01UnboundUnboundUnboundUnbound
1xvaA01UnboundAnalogue:ACTUnboundUnbound
1xvaB01UnboundAnalogue:ACTUnboundUnbound
1kiaA01UnboundAnalogue:ACTUnboundUnbound
1kiaB01UnboundAnalogue:ACTUnboundUnbound
1kiaC01UnboundAnalogue:ACTUnboundUnbound
1kiaD01UnboundAnalogue:ACTUnboundUnbound
1nbhA01UnboundAnalogue:ACTUnboundUnbound
1nbhB01UnboundAnalogue:ACTUnboundUnbound
1nbhC01UnboundAnalogue:ACTUnboundUnbound
1nbhD01UnboundAnalogue:ACTUnboundUnbound
1nbiA01UnboundUnboundUnboundUnbound
1nbiB01UnboundUnboundUnboundUnbound
1nbiC01UnboundUnboundUnboundUnbound
1nbiD01UnboundUnboundUnboundUnbound
1bhjA02UnboundUnboundUnboundUnbound
1bhjB02UnboundUnboundUnboundUnbound
1d2cA02UnboundUnboundUnboundUnbound
1d2cB02UnboundUnboundUnboundUnbound
1d2gA02UnboundUnboundUnboundUnbound
1d2gB02UnboundUnboundUnboundUnbound
1d2hA02UnboundUnboundBound:SAHUnbound
1d2hB02UnboundUnboundBound:SAHUnbound
1d2hC02UnboundUnboundBound:SAHUnbound
1d2hD02UnboundUnboundBound:SAHUnbound
1xvaA02Bound:SAMUnboundUnboundUnbound
1xvaB02Bound:SAMUnboundUnboundUnbound
1kiaA02Bound:SAMUnboundUnboundUnbound
1kiaB02Bound:SAMUnboundUnboundUnbound
1kiaC02Bound:SAMUnboundUnboundUnbound
1kiaD02Bound:SAMUnboundUnboundUnbound
1nbhA02Bound:SAMUnboundUnboundUnbound
1nbhB02Bound:SAMUnboundUnboundUnbound
1nbhC02Bound:SAMUnboundUnboundUnbound
1nbhD02Bound:SAMUnboundUnboundUnbound
1nbiA02Bound:SAMUnboundUnboundUnbound
1nbiB02Bound:SAMUnboundUnboundUnbound
1nbiC02Bound:SAMUnboundUnboundUnbound
1nbiD02Bound:SAMUnboundUnboundUnbound

Active-site residues
resource
literature [7]
pdbCatalytic residuesMain-chain involved in catalysiscomment
           
1bhjA01TYR 194
 
 
1bhjB01TYR 194
 
 
1d2cA01TYR 194
 
 
1d2cB01TYR 194
 
 
1d2gA01TYR 194
 
 
1d2gB01TYR 194
 
 
1d2hA01TYR 194
 
 
1d2hB01TYR 194
 
 
1d2hC01TYR 194
 
 
1d2hD01TYR 194
 
 
1xvaA01TYR 194
 
 
1xvaB01TYR 194
 
 
1kiaA01TYR 194
 
 
1kiaB01TYR 194
 
 
1kiaC01TYR 194
 
 
1kiaD01TYR 194
 
 
1nbhA01TYR 194
 
 
1nbhB01TYR 194
 
 
1nbhC01TYR 194
 
 
1nbhD01TYR 194
 
 
1nbiA01TYR 194
 
 
1nbiB01TYR 194
 
 
1nbiC01TYR 194
 
 
1nbiD01TYR 194
 
 
1bhjA02 
GLY 137
 
1bhjB02 
GLY 137
 
1d2cA02 
GLY 137
 
1d2cB02 
GLY 137
 
1d2gA02 
GLY 137
mutant R175K
1d2gB02 
GLY 137
mutant R175K
1d2hA02 
GLY 137
mutant R175K
1d2hB02 
GLY 137
mutant R175K
1d2hC02 
GLY 137
mutant R175K
1d2hD02 
GLY 137
mutant R175K
1xvaA02 
GLY 137
 
1xvaB02 
GLY 137
 
1kiaA02 
GLY 137
 
1kiaB02 
GLY 137
 
1kiaC02 
GLY 137
 
1kiaD02 
GLY 137
 
1nbhA02 
GLY 137
 
1nbhB02 
GLY 137
 
1nbhC02 
GLY 137
 
1nbhD02 
GLY 137
 
1nbiA02 
GLY 137
mutant R175K
1nbiB02 
GLY 137
mutant R175K
1nbiC02 
GLY 137
mutant R175K
1nbiD02 
GLY 137
mutant R175K

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]Fig.9, p.11992-119932
[3]Fig.6, p.212
[7]Fig.6, p.8399-8401

references
[1]
PubMed ID7734248
JournalJ Struct Biol
Year1994
Volume113
Pages247-9
AuthorsFu Z, Takusagawa F, Konishi K, Takata Y, Fujioka M
TitleCrystallization and preliminary X-ray diffraction studies of glycine methyltransferase from rat liver.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)
Medline ID96406816
PubMed ID8810903
JournalBiochemistry
Year1996
Volume35
Pages11985-93
AuthorsFu Z, Hu Y, Konishi K, Takata Y, Ogawa H, Gomi T, Fujioka M, Takusagawa F
TitleCrystal structure of glycine N-methyltransferase from rat liver.
Related PDB1xva
Related UniProtKBP13255
[3]
PubMed ID9597750
JournalInt J Biochem Cell Biol
Year1998
Volume30
Pages13-26
AuthorsOgawa H, Gomi T, Takusagawa F, Fujioka M
TitleStructure, function and physiological role of glycine N-methyltransferase.
[4]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
Medline ID98318042
PubMed ID9655336
JournalProtein Sci
Year1998
Volume7
Pages1326-31
AuthorsPattanayek R, Newcomer ME, Wagner C
TitleCrystal structure of apo-glycine N-methyltransferase (GNMT).
Related PDB1bhj
Related UniProtKBP13255
[5]
CommentsX-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS)
PubMed ID10756111
JournalJ Mol Biol
Year2000
Volume298
Pages149-62
AuthorsHuang Y, Komoto J, Konishi K, Takata Y, Ogawa H, Gomi T, Fujioka M, Takusagawa F
TitleMechanisms for auto-inhibition and forced product release in glycine N-methyltransferase: crystal structures of wild-type, mutant R175K and S-adenosylhomocysteine-bound R175K enzymes.
Related PDB1d2c,1d2g,1d2h
Related UniProtKBP13255
[6]
PubMed ID12079381
JournalJ Mol Biol
Year2002
Volume320
Pages223-35
AuthorsKomoto J, Huang Y, Takata Y, Yamada T, Konishi K, Ogawa H, Gomi T, Fujioka M, Takusagawa F
TitleCrystal structure of guanidinoacetate methyltransferase from rat liver: a model structure of protein arginine methyltransferase.
[7]
PubMed ID12859184
JournalBiochemistry
Year2003
Volume42
Pages8394-402
AuthorsTakata Y, Huang Y, Komoto J, Yamada T, Konishi K, Ogawa H, Gomi T, Fujioka M, Takusagawa F
TitleCatalytic mechanism of glycine N-methyltransferase.
Related PDB1nbh,1nbi


createdupdated
2004-03-172009-02-26


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