Protein Variants | Comment | Organism |
---|---|---|
C188S | the gene encoding UbaA C188S does not complement the ubaA knockout, revealing that Cys188 is likely to be important for the catalytic function of UbaA | Haloferax volcanii |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine | Haloferax volcanii | the enzyme is required for the formation of both SAMP1- and SAMP2-protein conjugates | AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine] | - |
? | |
ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine | Haloferax volcanii DSM 3757 | the enzyme is required for the formation of both SAMP1- and SAMP2-protein conjugates | AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine] | - |
? | |
ATP + [SAMP2]-Gly-Gly + [protein]-L-lysine | Haloferax volcanii | the enzyme is required for the formation of both SAMP1- and SAMP2-protein conjugates | AMP + diphosphate + N6-[[SAMP2]-Gly-Gly]-[[protein]-L-lysine] | - |
? | |
ATP + [SAMP2]-Gly-Gly + [protein]-L-lysine | Haloferax volcanii DSM 3757 | the enzyme is required for the formation of both SAMP1- and SAMP2-protein conjugates | AMP + diphosphate + N6-[[SAMP2]-Gly-Gly]-[[protein]-L-lysine] | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Haloferax volcanii | D4GSF3 | - |
- |
Haloferax volcanii DSM 3757 | D4GSF3 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
ATP + [SAMP]-Gly-Gly + [E1 SAMP-activating enzyme]-L-cysteine = S-[[SAMP]-Gly-Gly]-[[E1 SAMP-activating enzyme]-L-cysteine] + AMP + diphosphate | overall reaction | Haloferax volcanii | |
ATP + [SAMP]-Gly-Gly = diphosphate + [SAMP]-Gly-Gly-AMP | (1a) | Haloferax volcanii | |
[SAMP]-Gly-Gly-AMP + [E1 SAMP-activating enzyme]-L-cysteine = S-[[SAMP]-Gly-Gly]-[[E1 SAMP-activating enzyme]-L-cysteine] + AMP | (1b) | Haloferax volcanii |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine | the enzyme is required for the formation of both SAMP1- and SAMP2-protein conjugates | Haloferax volcanii | AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine] | - |
? | |
ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine | working model for archaea in which the E1-like UbaA and ubiquitin-like SAMP proteins function in both protein conjugation and sulfur transfer. In this model, UbaA catalyzes the adenylation of the C-terminal glycine of the SAMPs for their activation in protein conjugation. This adenylation would also activate SAMP1 and SAMP2 for their acceptance of sulfur as a C-terminal thiocarboxylate to serve as a sulfur carrier in MoCo biosynthesis and tRNA thiolation, respectively. During protein conjugation, a thioester intermediate is suggested to be formed between the active site Cys188 of UbaA and the C-terminal carboxyl group of the SAMPs. This prediction is based on: (i) the requirement of UbaA Cys188 for protein-conjugate formation, (ii) the conservation of UbaA Cys188 with the active site cysteine of E1-type enzymes known to form an E1-Ub thioester, and (iii) the detection of isopeptide (and not persulfide) bonds between the C-terminal carboxyl group of SAMP2 and the epsilon-amino group of lysine residues of target proteins. However, further studies are needed to demonstrate this intermediate. It is not clear whether UbaA forms a covalent intermediate with the SAMPs after their adenylation in the sulfur transfer pathways and what provides the activated source of sulfur for this putative thiocarboxylation reaction | Haloferax volcanii | AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine] | - |
? | |
ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine | the enzyme is required for the formation of both SAMP1- and SAMP2-protein conjugates | Haloferax volcanii DSM 3757 | AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine] | - |
? | |
ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine | working model for archaea in which the E1-like UbaA and ubiquitin-like SAMP proteins function in both protein conjugation and sulfur transfer. In this model, UbaA catalyzes the adenylation of the C-terminal glycine of the SAMPs for their activation in protein conjugation. This adenylation would also activate SAMP1 and SAMP2 for their acceptance of sulfur as a C-terminal thiocarboxylate to serve as a sulfur carrier in MoCo biosynthesis and tRNA thiolation, respectively. During protein conjugation, a thioester intermediate is suggested to be formed between the active site Cys188 of UbaA and the C-terminal carboxyl group of the SAMPs. This prediction is based on: (i) the requirement of UbaA Cys188 for protein-conjugate formation, (ii) the conservation of UbaA Cys188 with the active site cysteine of E1-type enzymes known to form an E1-Ub thioester, and (iii) the detection of isopeptide (and not persulfide) bonds between the C-terminal carboxyl group of SAMP2 and the epsilon-amino group of lysine residues of target proteins. However, further studies are needed to demonstrate this intermediate. It is not clear whether UbaA forms a covalent intermediate with the SAMPs after their adenylation in the sulfur transfer pathways and what provides the activated source of sulfur for this putative thiocarboxylation reaction | Haloferax volcanii DSM 3757 | AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine] | - |
? | |
ATP + [SAMP2]-Gly-Gly + [protein]-L-lysine | the enzyme is required for the formation of both SAMP1- and SAMP2-protein conjugates | Haloferax volcanii | AMP + diphosphate + N6-[[SAMP2]-Gly-Gly]-[[protein]-L-lysine] | - |
? | |
ATP + [SAMP2]-Gly-Gly + [protein]-L-lysine | working model for archaea in which the E1-like UbaA and ubiquitin-like SAMP proteins function in both protein conjugation and sulfur transfer. In this model, UbaA catalyzes the adenylation of the C-terminal glycine of the SAMPs for their activation in protein conjugation. This adenylation would also activate SAMP1 and SAMP2 for their acceptance of sulfur as a C-terminal thiocarboxylate to serve as a sulfur carrier in MoCo biosynthesis and tRNA thiolation, respectively. During protein conjugation, a thioester intermediate is suggested to be formed between the active site Cys188 of UbaA and the C-terminal carboxyl group of the SAMPs. This prediction is based on: (i) the requirement of UbaA Cys188 for protein-conjugate formation, (ii) the conservation of UbaA Cys188 with the active site cysteine of E1-type enzymes known to form an E1-Ub thioester, and (iii) the detection of isopeptide (and not persulfide) bonds between the C-terminal carboxyl group of SAMP2 and the epsilon-amino group of lysine residues of target proteins. However, further studies are needed to demonstrate this intermediate. It is not clear whether UbaA forms a covalent intermediate with the SAMPs after their adenylation in the sulfur transfer pathways and what provides the activated source of sulfur for this putative thiocarboxylation reaction | Haloferax volcanii | AMP + diphosphate + N6-[[SAMP2]-Gly-Gly]-[[protein]-L-lysine] | - |
? | |
ATP + [SAMP2]-Gly-Gly + [protein]-L-lysine | the enzyme is required for the formation of both SAMP1- and SAMP2-protein conjugates | Haloferax volcanii DSM 3757 | AMP + diphosphate + N6-[[SAMP2]-Gly-Gly]-[[protein]-L-lysine] | - |
? | |
ATP + [SAMP2]-Gly-Gly + [protein]-L-lysine | working model for archaea in which the E1-like UbaA and ubiquitin-like SAMP proteins function in both protein conjugation and sulfur transfer. In this model, UbaA catalyzes the adenylation of the C-terminal glycine of the SAMPs for their activation in protein conjugation. This adenylation would also activate SAMP1 and SAMP2 for their acceptance of sulfur as a C-terminal thiocarboxylate to serve as a sulfur carrier in MoCo biosynthesis and tRNA thiolation, respectively. During protein conjugation, a thioester intermediate is suggested to be formed between the active site Cys188 of UbaA and the C-terminal carboxyl group of the SAMPs. This prediction is based on: (i) the requirement of UbaA Cys188 for protein-conjugate formation, (ii) the conservation of UbaA Cys188 with the active site cysteine of E1-type enzymes known to form an E1-Ub thioester, and (iii) the detection of isopeptide (and not persulfide) bonds between the C-terminal carboxyl group of SAMP2 and the epsilon-amino group of lysine residues of target proteins. However, further studies are needed to demonstrate this intermediate. It is not clear whether UbaA forms a covalent intermediate with the SAMPs after their adenylation in the sulfur transfer pathways and what provides the activated source of sulfur for this putative thiocarboxylation reaction | Haloferax volcanii DSM 3757 | AMP + diphosphate + N6-[[SAMP2]-Gly-Gly]-[[protein]-L-lysine] | - |
? |
Synonyms | Comment | Organism |
---|---|---|
HVO_0558 | locus name | Haloferax volcanii |
UbaA | ubiquitin-activating E1 enzyme homolog of archaea | Haloferax volcanii |
General Information | Comment | Organism |
---|---|---|
malfunction | the ubaA mutant is deficient in SAMPylation with unconjugated Flag-SAMP1 and Flag-SAMP2 proteins. The ubaA knockout is complemented by providing a wild-type copy, but not a C188S variant of ubaA in trans. The ubaA mutant is retarded in growth at 50°C | Haloferax volcanii |
physiological function | the enzyme is required for the formation of both SAMP1- and SAMP2-protein conjugates. The enzyme can activate multiple ubiquitin-like proteins (SAMP1 and SAMP2) for protein conjugation as well as for sulfur transfer. In sulfur transfer, SAMP1 and SAMP2 appear specific for MoCo biosynthesis and the thiolation of tRNA, respectively | Haloferax volcanii |