Activating Compound | Comment | Organism | Structure |
---|---|---|---|
DMSO | levels of samp3ylated proteins and samp3 transcripts are increased by the addition of dimethyl sulfoxide to aerobically growing cells | Haloferax volcanii |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Haloferax volcanii |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine | Haloferax volcanii | - |
AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine] | - |
r | |
ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine | Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2 | - |
AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine] | - |
r | |
additional information | Haloferax volcanii | the molybdopterin (MPT) synthase large subunit homologue MoaE is samp3ylated at conserved active site lysine residues determined by MS/MS analysis, immunoprecipitation, and tandem affinity purifications. Samp3ylation is covalent and reversible and controls the activity of enzymes such as MPT synthase | ? | - |
? | |
additional information | Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2 | the molybdopterin (MPT) synthase large subunit homologue MoaE is samp3ylated at conserved active site lysine residues determined by MS/MS analysis, immunoprecipitation, and tandem affinity purifications. Samp3ylation is covalent and reversible and controls the activity of enzymes such as MPT synthase | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Haloferax volcanii | D4GSF3 | - |
- |
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2 | D4GSF3 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine | - |
Haloferax volcanii | AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine] | - |
r | |
ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine | SAMP3 from Haloferax volcanii strain H26 | Haloferax volcanii | AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine] | - |
r | |
ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine | - |
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2 | AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine] | - |
r | |
ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine | SAMP3 from Haloferax volcanii strain H26 | Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2 | AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine] | - |
r | |
additional information | the molybdopterin (MPT) synthase large subunit homologue MoaE is samp3ylated at conserved active site lysine residues determined by MS/MS analysis, immunoprecipitation, and tandem affinity purifications. Samp3ylation is covalent and reversible and controls the activity of enzymes such as MPT synthase | Haloferax volcanii | ? | - |
? | |
additional information | phylogenetic and sequence analysis and comparison of SAMP3 substrate, overview | Haloferax volcanii | ? | - |
? | |
additional information | the molybdopterin (MPT) synthase large subunit homologue MoaE is samp3ylated at conserved active site lysine residues determined by MS/MS analysis, immunoprecipitation, and tandem affinity purifications. Samp3ylation is covalent and reversible and controls the activity of enzymes such as MPT synthase | Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2 | ? | - |
? | |
additional information | phylogenetic and sequence analysis and comparison of SAMP3 substrate, overview | Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
E1 enzyme homologue | - |
Haloferax volcanii |
UbaA | - |
Haloferax volcanii |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Haloferax volcanii |
General Information | Comment | Organism |
---|---|---|
physiological function | the novel small archaeal modifier protein (SAMP3) with a beta-grasp fold and C-terminal diglycine motif characteristic of ubiquitin is functional in protein conjugation in Haloferax volcanii. Archaeal ubiquitin-like SAMP3 is isopeptide-linked to proteins via a UbaA-dependent mechanism. SAMP3 conjugates are dependent on the ubiquitin-activating E1 enzyme homologue of archaea (UbaA) for synthesis and are cleaved by the JAMM/MPN+ domain metalloprotease HvJAMM1. Samp3ylation is covalent and reversible and controls the activity of enzymes such as MPT synthase. Sampylation of MPT synthase may govern the levels of molybdenum cofactor available and thus facilitate the scavenging of oxygen prior to the transition to respiration with molybdenum-cofactor-containing terminal reductases that use alternative electron acceptors such as dimethyl sulfoxide | Haloferax volcanii |