S-adenosylmethionine-dependent methyltransferase (SAM-MTase or AdoMet-MTase) is a conserved protein domain and protein superfamily.[1] SAM-MTase proteins are methyltransferases.[2] There are five protein families within SAM-MTase,

SAM-dependent MTases superfamily
Cartoon representation of the molecular structure of the Crystal Structure of the SAM Dependent Methyltransferase from Agrobacterium tumefaciens (PDB: 2igt​)
Identifiers
SymbolSAM-dependent_MTases
ECOD2003.1.5
InterProIPR029063
AdoMet_MTase
Identifiers
SymbolAdoMet_MTase
PfamPF07757
Pfam clanCL0063
InterProIPR011671
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

SAM-MTases use S-adenosyl-L-methionine as a substrate for methylation, creating the product S-adenosyl-L-homocysteine.[3]

Structure and subgroups

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All SAM-MTases contain a structurally conserved SAM-binding domain consisting of a central seven-stranded beta-sheet that is flanked by three alpha-helices per side of the sheet.[4]

A review published in 2003 divides all methyltransferases into 5 main classes based on the structure of their catalytic domain (fold):[5]

  • class I: Rossmann-like α/β, the largest subgroup.[3]
  • class II: TIM β/α-barrel α/β
  • class III: tetrapyrrole methylase α/β
  • class IV: SPOUT α/β
  • class V: SET domain all β

References

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  1. ^ Wang, Jiyao; Chitsaz, Farideh; Derbyshire, Myra K.; Gonzales, Noreen R.; Gwadz, Marc; Lu, Shennan; Marchler, Gabriele H.; Song, James S.; Thanki, Narmada; Yamashita, Roxanne A.; Yang, Mingzhang; Zhang, Dachuan; Zheng, Chanjuan; Lanczycki, Christopher J.; Marchler-Bauer, Aron (2023-01-06). "The conserved domain database in 2023". Nucleic Acids Research. 51 (D1): D384–D388. doi:10.1093/nar/gkac1096. ISSN 1362-4962. PMC 9825596. PMID 36477806.
  2. ^ Knizewski L, Ginalski K (July 2006). "DUF1613 is a novel family of eucaryotic AdoMet-dependent methyltransferases". Cell Cycle. 5 (14): 1580–2. doi:10.4161/cc.5.14.2978. PMID 16861910.
  3. ^ a b "CDD Conserved Protein Domain Family: AdoMet_MTases". www.ncbi.nlm.nih.gov. Retrieved 2023-12-07.
  4. ^ Martin, Jennifer L; McMillan, Fiona M (2002-12-01). "SAM (dependent) I AM: the S-adenosylmethionine-dependent methyltransferase fold". Current Opinion in Structural Biology. 12 (6): 783–793. doi:10.1016/s0959-440x(02)00391-3. ISSN 1879-033X. PMID 12504684.
  5. ^ Schubert, Heidi L; Blumenthal, Robert M; Cheng, Xiaodong (2003-06-01). "Many paths to methyltransfer: a chronicle of convergence". Trends in Biochemical Sciences. 28 (6): 329–335. doi:10.1016/s0968-0004(03)00090-2. ISSN 0968-0004. PMC 2758044. PMID 12826405.
This article incorporates text from the public domain Pfam and InterPro: IPR011671
This article incorporates text from the public domain Pfam and InterPro: IPR029063