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2. Transferases

2.1 Transferring one-carbon groups

2.1.1 Methyltransferases

ID:	2.1.1.244
Description:	Protein N-terminal methyltransferase.
Cath:	3.40.50.150;

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UniProtKB Enzyme Link:	UniProtKB 2.1.1.244
BRENDA Enzyme Link:	BRENDA 2.1.1.244
KEGG Enzyme Link:	KEGG2.1.1.244
BioCyc Enzyme Link:	BioCyc 2.1.1.244
ExPASy Enzyme Link:	ExPASy2.1.1.244
EC2PDB Enzyme Link:	EC2PDB 2.1.1.244
ExplorEnz Enzyme Link:	ExplorEnz 2.1.1.244
PRIAM enzyme-specific profiles Link:	PRIAM 2.1.1.244
IntEnz Enzyme Link:	IntEnz 2.1.1.244
MEDLINE Enzyme Link:	MEDLINE 2.1.1.244

RHEA:54736	N-terminal L-prolyl-L-prolyl-L-lysyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N-terminal N,N-dimethyl-L-prolyl-L-prolyl-L-lysyl-[protein] + 2 S-adenosyl-L-homocysteine
RULE(radius=1)	[:1]-[NH;+0:2]-[:3].[:4]-[S+;H0:5](-[:6])-[CH3;+0:7].[:8]-[S+;H0:9](-[:10])-[CH3;+0:11]>>[:1]-[N+;H0:2](-[:3])(-[CH3;+0:11])-[CH3;+0:7].[:4]-[S;H0;+0:5]-[:6].[:8]-[S;H0;+0:9]-[:10]
Reaction
Core-to-Core	More

Title	Authors	Date	PubMed ID
Molecular basis for histone N-terminal methylation by NRMT1.	Wu R, Yue Y, Zheng X, Li H	2015 Nov 15	26543159
NRMT is an alpha-N-methyltransferase that methylates RCC1 and retinoblastoma protein.	Tooley CE, Petkowski JJ, Muratore-Schroeder TL, Balsbaugh JL, Shabanowitz J, Sabat M, Minor W, Hunt DF, Macara IG	2010 Aug 26	20668449

RHEA:54724	N-terminal L-seryl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N-terminal N,N,N-trimethyl-L-seryl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
RULE(radius=1)	[:1]-[NH2;+0:2].[:3]-[S+;H0:4](-[:5])-[CH3;+0:6].[:7]-[S+;H0:8](-[:9])-[CH3;+0:10].[:11]-[S+;H0:12](-[:13])-[CH3;+0:14]>>[:1]-[N+;H0:2](-[CH3;+0:10])(-[CH3;+0:14])-[CH3;+0:6].[:3]-[S;H0;+0:4]-[:5].[:7]-[S;H0;+0:8]-[:9].[:11]-[S;H0;+0:12]-[:13]
Reaction
Core-to-Core	No scaffolds atoms were exchanged as a result of the reaction

Title	Authors	Date	PubMed ID
Molecular basis for histone N-terminal methylation by NRMT1.	Wu R, Yue Y, Zheng X, Li H	2015 Nov 15	26543159
NRMT is an alpha-N-methyltransferase that methylates RCC1 and retinoblastoma protein.	Tooley CE, Petkowski JJ, Muratore-Schroeder TL, Balsbaugh JL, Shabanowitz J, Sabat M, Minor W, Hunt DF, Macara IG	2010 Aug 26	20668449

RHEA:54712	N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
RULE(radius=1)	[:1]-[NH2;+0:2].[:3]-[S+;H0:4](-[:5])-[CH3;+0:6].[:7]-[S+;H0:8](-[:9])-[CH3;+0:10].[:11]-[S+;H0:12](-[:13])-[CH3;+0:14]>>[:1]-[N+;H0:2](-[CH3;+0:10])(-[CH3;+0:14])-[CH3;+0:6].[:3]-[S;H0;+0:4]-[:5].[:7]-[S;H0;+0:8]-[:9].[:11]-[S;H0;+0:12]-[:13]
Reaction
Core-to-Core	No scaffolds atoms were exchanged as a result of the reaction

Title	Authors	Date	PubMed ID
Molecular basis for histone N-terminal methylation by NRMT1.	Wu R, Yue Y, Zheng X, Li H	2015 Nov 15	26543159
NRMT is an alpha-N-methyltransferase that methylates RCC1 and retinoblastoma protein.	Tooley CE, Petkowski JJ, Muratore-Schroeder TL, Balsbaugh JL, Shabanowitz J, Sabat M, Minor W, Hunt DF, Macara IG	2010 Aug 26	20668449