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Literature summary extracted from

  • Miranda, H.V.; Antelmann, H.; Hepowit, N.; Chavarria, N.E.; Krause, D.J.; Pritz, J.R.; Bไsell, K.; Becher, D.; Humbard, M.A.; Brocchieri, L.; Maupin-Furlow, J.A.
    Archaeal ubiquitin-like SAMP3 is isopeptide-linked to proteins via a UbaA-dependent mechanism (2013), Mol. Cell. Proteomics, 13, 220-239.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.19.15 EDTA inactivation Haloferax volcanii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.2.1.55 ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine Haloferax volcanii SAMP3 is a small protein modifier. It is suggested that samp3ylation regulates a variety of cellular functions including MoCo biosynthesis AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine]
-
 ?
6.2.1.55 ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine Haloferax volcanii DSM 3757 SAMP3 is a small protein modifier. It is suggested that samp3ylation regulates a variety of cellular functions including MoCo biosynthesis AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine]
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.19.15 Haloferax volcanii D4GTS4
-
-
3.4.19.15 Haloferax volcanii DSM 3757 D4GTS4
-
-
6.2.1.55 Haloferax volcanii D4GSF3
-
-
6.2.1.55 Haloferax volcanii DSM 3757 D4GSF3
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.19.15 additional information JAMM1 is a metalloprotease with relatively broad substrate specificity, able to cleave a wide variety of proteins conjugated to SAMP3 as well as SAMP1/2 Haloferax volcanii ?
-
 ?
3.4.19.15 additional information JAMM1 is a metalloprotease with relatively broad substrate specificity, able to cleave a wide variety of proteins conjugated to SAMP3 as well as SAMP1/2 Haloferax volcanii DSM 3757 ?
-
 ?
3.4.19.15 N6-[SAMP3]-[MoaE]-L-lysine + H2O MoaE, i.e. molybdopterin synthase large subunit homolog Haloferax volcanii [MoaE]-L-lysine + SAMP3 SAMP3 protein conjugates are dependent on the ubiquitin-activating E1 enzyme homolog of archaea (UbaA) for synthesis and are cleaved by the JAMM/MPN+ domain metalloprotease JAMM1 ?
3.4.19.15 N6-[SAMP3]-[MoaE]-L-lysine + H2O MoaE, i.e. molybdopterin synthase large subunit homolog Haloferax volcanii DSM 3757 [MoaE]-L-lysine + SAMP3 SAMP3 protein conjugates are dependent on the ubiquitin-activating E1 enzyme homolog of archaea (UbaA) for synthesis and are cleaved by the JAMM/MPN+ domain metalloprotease JAMM1 ?
6.2.1.55 ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine SAMP3 is a small protein modifier. It is suggested that samp3ylation regulates a variety of cellular functions including MoCo biosynthesis Haloferax volcanii AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine]
-
 ?
6.2.1.55 ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine SAMP3 conjugates are dependent on the C-terminal diglycine motif of SAMP3 and the ubiquitin-activating E1 enzyme homolog of archaea (UbaA) for synthesis. Samp3ylation is dependent on UbaA and forms covalent isopeptide bonds between the C-terminal carboxylate of SAMP3 and the epsilon-amino group of lysine residues of protein targets. No common motif in primary amino acid sequence or secondary structure of the samp3ylation sites is detected. The K240 and K247 residues of the MoaE-MobB domain protein HVO_1864 (named MoaE) are demonstrated to be samp3ylated are also known to be samp1ylated. The translation elongation factor EF-1 alpha homolog HVO_0359 is found to be samp3ylated at K99. polySAMP3 chains form in the cell. In particular, the C-terminal carboxylate of SAMP3 is isopeptide linked to at least three (K18, K55, and K62) of its three lysine residues in all biological replicates Haloferax volcanii AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine]
-
 ?
6.2.1.55 ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine SAMP3 is a small protein modifier. It is suggested that samp3ylation regulates a variety of cellular functions including MoCo biosynthesis Haloferax volcanii DSM 3757 AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine]
-
 ?
6.2.1.55 ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine SAMP3 conjugates are dependent on the C-terminal diglycine motif of SAMP3 and the ubiquitin-activating E1 enzyme homolog of archaea (UbaA) for synthesis. Samp3ylation is dependent on UbaA and forms covalent isopeptide bonds between the C-terminal carboxylate of SAMP3 and the epsilon-amino group of lysine residues of protein targets. No common motif in primary amino acid sequence or secondary structure of the samp3ylation sites is detected. The K240 and K247 residues of the MoaE-MobB domain protein HVO_1864 (named MoaE) are demonstrated to be samp3ylated are also known to be samp1ylated. The translation elongation factor EF-1 alpha homolog HVO_0359 is found to be samp3ylated at K99. polySAMP3 chains form in the cell. In particular, the C-terminal carboxylate of SAMP3 is isopeptide linked to at least three (K18, K55, and K62) of its three lysine residues in all biological replicates Haloferax volcanii DSM 3757 AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine]
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.19.15 HVO_2505
-
 Haloferax volcanii
3.4.19.15 JAMM1
-
 Haloferax volcanii
6.2.1.55 HVO_0558 locus name Haloferax volcanii
6.2.1.55 UbaA ubiquitin-activating E1 enzyme homolog of archaea Haloferax volcanii

General Information

EC Number General Information Comment Organism
6.2.1.55 malfunction no samp3ylation is detected in the DELTAubaA mutant Haloferax volcanii