AdoMet MTase
{{Short description|Protein domain and superfamily}}
{{Infobox protein family
| Symbol = SAM-dependent_MTases
| Name = SAM-dependent MTases superfamily
| image = File:PDB 2igt EBI.jpg
| width =
| caption = Cartoon representation of the molecular structure of the [https://www.ebi.ac.uk/pdbe/entry/pdb/2igt Crystal Structure of the SAM Dependent Methyltransferase from Agrobacterium tumefaciens] ({{PDB|2igt}})
| Pfam =
| Pfam_clan =
| ECOD = 2003.1.5
| InterPro = IPR029063
| SMART =
| PROSITE =
| MEROPS =
| SCOP =
| TCDB =
| OPM family =
| OPM protein =
| CAZy =
| CDD =
}}
{{Infobox protein family
| Symbol = AdoMet_MTase
| Name = AdoMet_MTase
| image =
| width =
| caption =
| Pfam = PF07757
| Pfam_clan = CL0063
| InterPro = IPR011671
| SMART =
| PROSITE =
| MEROPS =
| SCOP =
| TCDB =
| OPM family =
| OPM protein =
| CAZy =
| CDD =
}}
S-adenosylmethionine-dependent methyltransferase (SAM-MTase or AdoMet-MTase) is a conserved protein domain and protein superfamily.{{Cite journal |last1=Wang |first1=Jiyao |last2=Chitsaz |first2=Farideh |last3=Derbyshire |first3=Myra K. |last4=Gonzales |first4=Noreen R. |last5=Gwadz |first5=Marc |last6=Lu |first6=Shennan |last7=Marchler |first7=Gabriele H. |last8=Song |first8=James S. |last9=Thanki |first9=Narmada |last10=Yamashita |first10=Roxanne A. |last11=Yang |first11=Mingzhang |last12=Zhang |first12=Dachuan |last13=Zheng |first13=Chanjuan |last14=Lanczycki |first14=Christopher J. |last15=Marchler-Bauer |first15=Aron |date=2023-01-06 |title=The conserved domain database in 2023 |journal=Nucleic Acids Research |volume=51 |issue=D1 |pages=D384–D388 |doi=10.1093/nar/gkac1096 |issn=1362-4962 |pmc=9825596 |pmid=36477806}} SAM-MTase proteins are methyltransferases.{{cite journal |vauthors=Knizewski L, Ginalski K |date=July 2006 |title=DUF1613 is a novel family of eucaryotic AdoMet-dependent methyltransferases |journal=Cell Cycle |volume=5 |issue=14 |pages=1580–2 |doi=10.4161/cc.5.14.2978 |pmid=16861910 |doi-access=free}} There are five protein families within SAM-MTase,
SAM-MTases use S-adenosyl-L-methionine as a substrate for methylation, creating the product S-adenosyl-L-homocysteine.{{Cite web |title=CDD Conserved Protein Domain Family: AdoMet_MTases |url=https://www.ncbi.nlm.nih.gov/Structure/cdd/cl17173 |access-date=2023-12-07 |website=www.ncbi.nlm.nih.gov}}
Structure and subgroups
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.{{Cite journal |last1=Martin |first1=Jennifer L |last2=McMillan |first2=Fiona M |date=2002-12-01 |title=SAM (dependent) I AM: the S-adenosylmethionine-dependent methyltransferase fold |url=https://doi.org/10.1016/s0959-440x(02)00391-3 |journal=Current Opinion in Structural Biology |volume=12 |issue=6 |pages=783–793 |doi=10.1016/s0959-440x(02)00391-3 |issn=1879-033X |pmid=12504684|url-access=subscription }}
A review published in 2003 divides all methyltransferases into 5 main classes based on the structure of their catalytic domain (fold):{{Cite journal |last1=Schubert |first1=Heidi L |last2=Blumenthal |first2=Robert M |last3=Cheng |first3=Xiaodong |date=2003-06-01 |title=Many paths to methyltransfer: a chronicle of convergence |journal=Trends in Biochemical Sciences |volume=28 |issue=6 |pages=329–335 |doi=10.1016/s0968-0004(03)00090-2 |issn=0968-0004 |pmc=2758044 |pmid=12826405}}
References
{{reflist}}
{{InterPro content|IPR011671}}
{{InterPro content|IPR029063}}
{{Chemistry-stub}}