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Literature summary for 6.2.1.55 extracted from

  • Hepowit, N.; de Vera, I.; Cao, S.; Fu, X.; Wu, Y.; Uthandi, S.; Chavarria, N.; Englert, M.; Su, D.; Sӧll, D.; Kojetin, D.; Maupin-Furlow, J.
    Mechanistic insight into protein modification and sulfur mobilization activities of noncanonical E1 and associated ubiquitin-like proteins of archaea (2016), FEBS J., 183, 3567-3586 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.2.1.55

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetics and thermodynamics of the enzyme with wild-type and mutant SAMP substrates, overview Haloferax volcanii

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Haloferax volcanii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + [SAMP1]-Gly-Gly + [UbaA]-L-cysteine Haloferax volcanii
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 AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[UbaA]-L-cysteine]
-
 ?
ATP + [SAMP1]-Gly-Gly + [UbaA]-L-cysteine Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
 AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[UbaA]-L-cysteine]
-
 ?
ATP + [SAMP2]-Gly-Gly + [UbaA]-L-cysteine Haloferax volcanii
-
 AMP + diphosphate + N6-[[SAMP2]-Gly-Gly]-[[UbaA]-L-cysteine]
-
 ?
ATP + [SAMP2]-Gly-Gly + [UbaA]-L-cysteine Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
 AMP + diphosphate + N6-[[SAMP2]-Gly-Gly]-[[UbaA]-L-cysteine]
-
 ?
ATP + [SAMP3]-Gly-Gly + [UbaA]-L-cysteine Haloferax volcanii
-
 AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[UbaA]-L-cysteine]
-
 ?
ATP + [SAMP3]-Gly-Gly + [UbaA]-L-cysteine Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
 AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[UbaA]-L-cysteine]
-
 ?

Organism

Organism UniProt Comment Textmining
Haloferax volcanii D4GSF3
-
-
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2 D4GSF3
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information UbaA is ubiquitin-like-automodified at lysine residues required for early (ATP binding) and late (sulfur mobilization) stages of enzyme activity revealing multiple layers of autoregulation. Cysteine residues, distinct from the canonical E1 active site cysteine, are found important in UbaA function supporting a model that this non-canonical E1 is structurally flexible in its active site to allow Ubl-adenylate, Ubl-E1-like thioester and cysteine persulfide(s) intermediates to form. Thermodynamics of Ubl protein binding, thioester intermediate, regulation by auto-modification, and amino acid residues important for catalytic function, overview. UbaA is autosampylated, autosampylation of K87 and K157 likely regulates UbaA function Haloferax volcanii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + [SAMP1]-Gly-Gly + [UbaA]-L-cysteine
-
 Haloferax volcanii AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[UbaA]-L-cysteine]
-
 ?
ATP + [SAMP1]-Gly-Gly + [UbaA]-L-cysteine
-
 Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2 AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[UbaA]-L-cysteine]
-
 ?
ATP + [SAMP2]-Gly-Gly + [UbaA]-L-cysteine
-
 Haloferax volcanii AMP + diphosphate + N6-[[SAMP2]-Gly-Gly]-[[UbaA]-L-cysteine]
-
 ?
ATP + [SAMP2]-Gly-Gly + [UbaA]-L-cysteine
-
 Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2 AMP + diphosphate + N6-[[SAMP2]-Gly-Gly]-[[UbaA]-L-cysteine]
-
 ?
ATP + [SAMP3]-Gly-Gly + [UbaA]-L-cysteine
-
 Haloferax volcanii AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[UbaA]-L-cysteine]
-
 ?
ATP + [SAMP3]-Gly-Gly + [UbaA]-L-cysteine
-
 Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2 AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[UbaA]-L-cysteine]
-
 ?
additional information ATP hydrolysis triggers the formation of thioester and peptide bonds within the Ubl:E1-like complex. Structure-function relationships of the archaeal UbaA/SAMPs, overview. UbaA binds the nucleotide ligands AMP-PNP, ATP and ADP but not AMP, CTP, GTP, UTP, and TTP. Diphosphate is released when UbaA is incubated with SAMPs and ATP, but not with the other nucleoside triphosphates Haloferax volcanii ?
-
 ?
additional information ATP hydrolysis triggers the formation of thioester and peptide bonds within the Ubl:E1-like complex. Structure-function relationships of the archaeal UbaA/SAMPs, overview. UbaA binds the nucleotide ligands AMP-PNP, ATP and ADP but not AMP, CTP, GTP, UTP, and TTP. Diphosphate is released when UbaA is incubated with SAMPs and ATP, but not with the other nucleoside triphosphates Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2 ?
-
 ?

Synonyms

Synonyms Comment Organism
E1-like enzyme
-
 Haloferax volcanii
non-canonical E1
-
 Haloferax volcanii
noncanonical E1
-
 Haloferax volcanii
noncanonical E1-like enzyme
-
 Haloferax volcanii
UbaA
-
 Haloferax volcanii

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 ATP and its non-hydrolyzable analogue AMP-PNP have the greatest influence on the Tm of UbaA (with an increase of 8.2°C and 7.4°C, respectively). ADP also increases the Tm of UbaA (by 4.4°C), whereas AMP, CTP, GTP, UTP, and TTP have no detectable effect in these assays Haloferax volcanii

Cofactor

Cofactor Comment Organism Structure
ATP ATP hydrolysis triggers the formation of thioester and peptide bonds within the Ubl:E1-like complex, docking of ATP Haloferax volcanii

General Information

General Information Comment Organism
evolution ancestral relatives of Ub/E1 are identified that mobilize sulfur to form sulfur-containing biomolecules (e.g. thiamine, molybdopterin (MPT), thiolated tRNA, thiol-functionalized siderophores, and 2-thiosugars). In bacteria, these E1-like enzymes adenylate and activate the C-terminus of the Ub-like (Ubl) protein by hydrolyzing ATP and releasing diphosphate. Comparison of E1/MoeB/ThiF superfamily proteins. UbaA contains no rhodaneses (RHD) domain Haloferax volcanii
additional information key residues within the adenylation domain of UbaA are needed to bind ATP, discovery of residues that are specifically needed to catalyze the downstream reactions of sulfur mobilization and/or Ubl protein modification, overview. The enzyme has an active site cysteine residue, Cys188, that is critical for the sulfurtransferase activity, but not needed to form the thiol-intermediate or Ubl-bonds, also residue K159 is not required for ubiquitin-like bond formation. Residues C171 and C245 of the Cys tetrade and residues K87 and D131 are all required for all enzyme activities, while C174 and C248 are not essential, Residue C265 is needed for the thiolation of wobble uridine tRNA. Residue R74 is not critical for the sulfurtransferase activity, but needed to form Ubl-bonds. Residue N71 is required for thiolation of tRNA, sulfurtransferase, and Ubl bond formation activities. Residues K87 and K157 are autosampylated Haloferax volcanii
physiological function in bacteria, these E1-like enzymes adenylate and activate the C-terminus of the Ub-like (Ubl) protein by hydrolyzing ATP and releasing diphosphate. Protein modification and sulfur mobilization activities of noncanonical E1 and associated ubiquitin-like (Ubl) proteins of archaea, overview. Enzyme UbaA is autoregulated by Ubl-protein modification and structurally flexible to allow Ubl-adenylate, Ubl-E1 thioester and persulfide(s) intermediates to form in the absence of a canonical E1 active site cysteine. Autosampylation of K87 and K157 likely regulates UbaA function Haloferax volcanii