A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.
ENZYME entry: EC 184.108.40.206
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|SAMP-activating enzyme E1.|
|ATP + [SAMP]-Gly-Gly <=> diphosphate + [SAMP]-Gly-Gly-AMP|
- The enzyme catalyzes the activation of SAMPs (Small Archaeal Modifier
Proteins), which are ubiquitin-like proteins found only in the
Archaea, by catalyzing the ATP-dependent formation of a SAMP
adenylate in which the C-terminal glycine of SAMP is bound to AMP via
an acyl-phosphate linkage.
- The product of this activity can accept a sulfur atom to form a
thiocarboxylate moiety that acts as a sulfur carrier involved in
thiolation of tRNA and other metabolites such as molybdopterin.
- Alternatively, the enzyme can also catalyze the transfer of SAMP from
its activated form to an internal cysteine residue, leading to a
process termed SAMPylation (see EC 220.127.116.11).
|PRIAM enzyme-specific profiles||18.104.22.168|
|KEGG Ligand Database for Enzyme Nomenclature||22.214.171.124|
|IUBMB Enzyme Nomenclature||126.96.36.199|
|MEDLINE||Find literature relating to 188.8.131.52|
entries corresponding to 2.7.7.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.7.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.-.-.-