Any feedback?
Information on EC 6.2.1.55 - E1 SAMP-activating enzyme
for references in articles please use BRENDA:EC6.2.1.55Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
6.2.1.55 E1 SAMP-activating enzymeIUBMB Comments
Contains Zn2+. The enzyme catalyses the activation of SAMPs (Small Archaeal Modifier Proteins), which are ubiquitin-like proteins found only in the Archaea. SAMPs are involved in protein degradation, and also act as sulfur carriers involved in thiolation of tRNA and other metabolites such as molybdopterin. The enzyme catalyses the ATP-dependent formation of a SAMP adenylate intermediate in which the C-terminal glycine of SAMP is bound to AMP via an acyl-phosphate linkage (reaction 1). This intermediate can accept a sulfur atom to form a thiocarboxylate moiety in a mechanism that is not yet understood. Alternatively, the E1 enzyme can transfer SAMP from its activated form to an internal cysteine residue, releasing AMP (reaction 2). In this case SAMP is subsequently transferred to a lysine residue in a target protein in a process termed SAMPylation. Auto-SAMPylation (attachment of SAMP to lysine residues within the E1 enzyme) has been observed. cf. EC 2.7.7.100, SAMP-activating enzyme.
Specify your search results
Word Map
- 6.2.1.55
-
ubiquitin-like
-
e2-like
-
autophagosome
-
autophagy-related
- volcanii
-
haloferax
-
sampylation
- ufm1
-
urmylation
-
apg12p
- samp1
- molybdopterin
-
cytoplasm-to-vacuole
-
ubiquitin-related
-
lc3-lipidation
-
ubiquitin-fold
-
gabarap
The expected taxonomic range for this enzyme is: Haloferax volcanii
Reaction Schemes
+
+
=
+
+
+
[SAMP]-Gly-Gly
+
[E1 SAMP-activating enzyme]-L-cysteine
=
+
+
+
[SAMP]-Gly-Gly
=
+
[SAMP]-Gly-Gly-AMP
+
=
+
[SAMP]-Gly-Gly-AMP
+
[E1 SAMP-activating enzyme]-L-cysteine
=
+
Synonyms
e1-like enzyme, noncanonical e1, e1-like ubaa, non-canonical e1, samp-activating e1 enzyme, noncanonical e1-like enzyme, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E1 enzyme homologue
E1-like enzyme
E1-like UbaA
HVO_0558
non-canonical E1
noncanonical E1
noncanonical E1-like enzyme
SAMP-activating E1 enzyme
UbaA
E1 enzyme homologue
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
-
E1-like enzyme
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
-
E1-like UbaA
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
-
non-canonical E1
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
-
noncanonical E1
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
-
noncanonical E1-like enzyme
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
-
SAMP-activating E1 enzyme
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
-
UbaA
ubiquitin-activating E1 enzyme homolog of archaea
UbaA
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + [SAMP]-Gly-Gly + [E1 SAMP-activating enzyme]-L-cysteine = S-[[SAMP]-Gly-Gly]-[[E1 SAMP-activating enzyme]-L-cysteine] + AMP + diphosphate
[SAMP]-Gly-Gly-AMP + [E1 SAMP-activating enzyme]-L-cysteine = S-[[SAMP]-Gly-Gly]-[[E1 SAMP-activating enzyme]-L-cysteine] + AMP
ATP + [SAMP]-Gly-Gly + [E1 SAMP-activating enzyme]-L-cysteine = S-[[SAMP]-Gly-Gly]-[[E1 SAMP-activating enzyme]-L-cysteine] + AMP + diphosphate
overall reaction
ATP + [SAMP]-Gly-Gly + [E1 SAMP-activating enzyme]-L-cysteine = S-[[SAMP]-Gly-Gly]-[[E1 SAMP-activating enzyme]-L-cysteine] + AMP + diphosphate
overall reaction
-
-
ATP + [SAMP]-Gly-Gly + [E1 SAMP-activating enzyme]-L-cysteine = S-[[SAMP]-Gly-Gly]-[[E1 SAMP-activating enzyme]-L-cysteine] + AMP + diphosphate
-
-
-
-
ATP + [SAMP]-Gly-Gly = diphosphate + [SAMP]-Gly-Gly-AMP
-
-
-
-
[SAMP]-Gly-Gly-AMP + [E1 SAMP-activating enzyme]-L-cysteine = S-[[SAMP]-Gly-Gly]-[[E1 SAMP-activating enzyme]-L-cysteine] + AMP
(1b)
[SAMP]-Gly-Gly-AMP + [E1 SAMP-activating enzyme]-L-cysteine = S-[[SAMP]-Gly-Gly]-[[E1 SAMP-activating enzyme]-L-cysteine] + AMP
(1b)
-
-
[SAMP]-Gly-Gly-AMP + [E1 SAMP-activating enzyme]-L-cysteine = S-[[SAMP]-Gly-Gly]-[[E1 SAMP-activating enzyme]-L-cysteine] + AMP
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
[SAMP]:[E1 SAMP-activating enzyme] ligase (AMP-forming)
Contains Zn2+. The enzyme catalyses the activation of SAMPs (Small Archaeal Modifier Proteins), which are ubiquitin-like proteins found only in the Archaea. SAMPs are involved in protein degradation, and also act as sulfur carriers involved in thiolation of tRNA and other metabolites such as molybdopterin. The enzyme catalyses the ATP-dependent formation of a SAMP adenylate intermediate in which the C-terminal glycine of SAMP is bound to AMP via an acyl-phosphate linkage (reaction 1). This intermediate can accept a sulfur atom to form a thiocarboxylate moiety in a mechanism that is not yet understood. Alternatively, the E1 enzyme can transfer SAMP from its activated form to an internal cysteine residue, releasing AMP (reaction 2). In this case SAMP is subsequently transferred to a lysine residue in a target protein in a process termed SAMPylation. Auto-SAMPylation (attachment of SAMP to lysine residues within the E1 enzyme) has been observed. cf. EC 2.7.7.100, SAMP-activating enzyme.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine]
ATP + [SAMP1]-Gly-Gly + [UbaA]-L-cysteine
AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[UbaA]-L-cysteine]
ATP + [SAMP2]-Gly-Gly + [NcsA protein]-L-lysine
AMP + diphosphate + N6-[[SAMP2]-Gly-Gly]-[[NcsA protein]-L-lysine]
ATP + [SAMP2]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP2]-Gly-Gly]-[[protein]-L-lysine]
ATP + [SAMP2]-Gly-Gly + [UbaA]-L-cysteine
AMP + diphosphate + N6-[[SAMP2]-Gly-Gly]-[[UbaA]-L-cysteine]
ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine]
ATP + [SAMP3]-Gly-Gly + [UbaA]-L-cysteine
AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[UbaA]-L-cysteine]
ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine]
-
-
-
?
ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine]
the enzyme is required for the formation of both SAMP1- and SAMP2-protein conjugates
-
-
?
ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine]
Haloferax volcanii forms differential SAMP-conjugates in the presence of only a single E1 and in the absence of any apparent E2 or E3 homologues suggesting a streamlined ubiquitin-like system for protein conjugation
-
-
?
ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[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
-
-
?
ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine]
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
-
-
?
ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine]
Haloferax volcanii forms differential SAMP-conjugates in the presence of only a single E1 and in the absence of any apparent E2 or E3 homologues suggesting a streamlined ubiquitin-like system for protein conjugation
-
-
?
ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine]
the enzyme is required for the formation of both SAMP1- and SAMP2-protein conjugates
-
-
?
ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[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
-
-
?
ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine]
Haloferax volcanii YW1001
-
-
-
-
?
ATP + [SAMP1]-Gly-Gly + [UbaA]-L-cysteine
AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[UbaA]-L-cysteine]
-
-
-
?
ATP + [SAMP1]-Gly-Gly + [UbaA]-L-cysteine
AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[UbaA]-L-cysteine]
-
-
-
-
?
ATP + [SAMP1]-Gly-Gly + [UbaA]-L-cysteine
AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[UbaA]-L-cysteine]
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
-
-
?
ATP + [SAMP1]-Gly-Gly + [UbaA]-L-cysteine
AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[UbaA]-L-cysteine]
Haloferax volcanii YW1001
-
-
-
-
?
ATP + [SAMP2]-Gly-Gly + [NcsA protein]-L-lysine
AMP + diphosphate + N6-[[SAMP2]-Gly-Gly]-[[NcsA protein]-L-lysine]
NcsA is an archaeal homolog of the cytoplasmic tRNA 2-thiolation protein 1 (Tuc1/Ncs6). NcsA is essential for growth at high temperature and required for formation of thiolated tRNALys UUU. NcsA is modified at Lys204 by isopeptide linkage to polymeric chains of the ubiquitin-fold protein SAMP2
-
-
?
ATP + [SAMP2]-Gly-Gly + [NcsA protein]-L-lysine
AMP + diphosphate + N6-[[SAMP2]-Gly-Gly]-[[NcsA protein]-L-lysine]
NcsA is an archaeal homolog of the cytoplasmic tRNA 2-thiolation protein 1 (Tuc1/Ncs6). NcsA is essential for growth at high temperature and required for formation of thiolated tRNALys UUU. NcsA is modified at Lys204 by isopeptide linkage to polymeric chains of the ubiquitin-fold protein SAMP2
-
-
?
ATP + [SAMP2]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP2]-Gly-Gly]-[[protein]-L-lysine]
the enzyme is required for the formation of both SAMP1- and SAMP2-protein conjugates
-
-
?
ATP + [SAMP2]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP2]-Gly-Gly]-[[protein]-L-lysine]
Haloferax volcanii forms differential SAMP-conjugates in the presence of only a single E1 and in the absence of any apparent E2 or E3 homologues suggesting a streamlined ubiquitin-like system for protein conjugation
-
-
?
ATP + [SAMP2]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[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
-
-
?
ATP + [SAMP2]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP2]-Gly-Gly]-[[protein]-L-lysine]
Haloferax volcanii forms differential SAMP-conjugates in the presence of only a single E1 and in the absence of any apparent E2 or E3 homologues suggesting a streamlined ubiquitin-like system for protein conjugation
-
-
?
ATP + [SAMP2]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP2]-Gly-Gly]-[[protein]-L-lysine]
the enzyme is required for the formation of both SAMP1- and SAMP2-protein conjugates
-
-
?
ATP + [SAMP2]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[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
-
-
?
ATP + [SAMP2]-Gly-Gly + [UbaA]-L-cysteine
AMP + diphosphate + N6-[[SAMP2]-Gly-Gly]-[[UbaA]-L-cysteine]
-
-
-
?
ATP + [SAMP2]-Gly-Gly + [UbaA]-L-cysteine
AMP + diphosphate + N6-[[SAMP2]-Gly-Gly]-[[UbaA]-L-cysteine]
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
-
-
?
ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine]
-
-
-
?
ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine]
-
-
-
r
ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[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
-
-
?
ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[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
-
-
?
ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine]
SAMP3 from Haloferax volcanii strain H26
-
-
r
ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine]
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
-
-
r
ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine]
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
SAMP3 from Haloferax volcanii strain H26
-
-
r
ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine]
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
-
-
?
ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[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
-
-
?
ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[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
-
-
?
ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine]
Haloferax volcanii YW1001
-
-
-
-
?
ATP + [SAMP3]-Gly-Gly + [UbaA]-L-cysteine
AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[UbaA]-L-cysteine]
-
-
-
?
ATP + [SAMP3]-Gly-Gly + [UbaA]-L-cysteine
AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[UbaA]-L-cysteine]
-
-
-
-
?
ATP + [SAMP3]-Gly-Gly + [UbaA]-L-cysteine
AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[UbaA]-L-cysteine]
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
-
-
?
additional information
?
-
many of the sampylated proteins that are identified (from cells grown aerobically on DMSO) are homologues of sulfur metabolism, oxidative stress, and/or autoregulation. Proteins found multiply modified by sampylation are examples of this association including the E1-like UbaA, the ubiquitin-like SAMP3 (related to SAMP1), the large subunit of MPT synthase (MoaE), and a methionine sulfoxide-S-reductase homologue (MsrA)
-
-
?
additional information
?
-
-
many of the sampylated proteins that are identified (from cells grown aerobically on DMSO) are homologues of sulfur metabolism, oxidative stress, and/or autoregulation. Proteins found multiply modified by sampylation are examples of this association including the E1-like UbaA, the ubiquitin-like SAMP3 (related to SAMP1), the large subunit of MPT synthase (MoaE), and a methionine sulfoxide-S-reductase homologue (MsrA)
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
phylogenetic and sequence analysis and comparison of SAMP3 substrate, overview
-
-
?
additional information
?
-
the SAMP1 S85R variant is found functional in sulfur mobilization and isopeptide linkage. Addition of DMSO to the culture medium increased the diversity of SAMP1 S85R conjugates in a banding pattern that is comparable to wild-type but distinct from SAMP1 S85K. Of the SAMPs encoded on the genome of Haloferax volcanii, only SAMP2 has a native (R/K) preceding the C-terminal di-Gly motif
-
-
?
additional information
?
-
-
the SAMP1 S85R variant is found functional in sulfur mobilization and isopeptide linkage. Addition of DMSO to the culture medium increased the diversity of SAMP1 S85R conjugates in a banding pattern that is comparable to wild-type but distinct from SAMP1 S85K. Of the SAMPs encoded on the genome of Haloferax volcanii, only SAMP2 has a native (R/K) preceding the C-terminal di-Gly motif
-
-
?
additional information
?
-
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
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
-
-
?
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
-
-
?
additional information
?
-
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
phylogenetic and sequence analysis and comparison of SAMP3 substrate, overview
-
-
?
additional information
?
-
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
many of the sampylated proteins that are identified (from cells grown aerobically on DMSO) are homologues of sulfur metabolism, oxidative stress, and/or autoregulation. Proteins found multiply modified by sampylation are examples of this association including the E1-like UbaA, the ubiquitin-like SAMP3 (related to SAMP1), the large subunit of MPT synthase (MoaE), and a methionine sulfoxide-S-reductase homologue (MsrA)
-
-
?
additional information
?
-
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
the SAMP1 S85R variant is found functional in sulfur mobilization and isopeptide linkage. Addition of DMSO to the culture medium increased the diversity of SAMP1 S85R conjugates in a banding pattern that is comparable to wild-type but distinct from SAMP1 S85K. Of the SAMPs encoded on the genome of Haloferax volcanii, only SAMP2 has a native (R/K) preceding the C-terminal di-Gly motif
-
-
?
additional information
?
-
Haloferax volcanii YW1001
-
many of the sampylated proteins that are identified (from cells grown aerobically on DMSO) are homologues of sulfur metabolism, oxidative stress, and/or autoregulation. Proteins found multiply modified by sampylation are examples of this association including the E1-like UbaA, the ubiquitin-like SAMP3 (related to SAMP1), the large subunit of MPT synthase (MoaE), and a methionine sulfoxide-S-reductase homologue (MsrA)
-
-
?
additional information
?
-
Haloferax volcanii YW1001
-
the SAMP1 S85R variant is found functional in sulfur mobilization and isopeptide linkage. Addition of DMSO to the culture medium increased the diversity of SAMP1 S85R conjugates in a banding pattern that is comparable to wild-type but distinct from SAMP1 S85K. Of the SAMPs encoded on the genome of Haloferax volcanii, only SAMP2 has a native (R/K) preceding the C-terminal di-Gly motif
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine]
ATP + [SAMP1]-Gly-Gly + [UbaA]-L-cysteine
AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[UbaA]-L-cysteine]
ATP + [SAMP2]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP2]-Gly-Gly]-[[protein]-L-lysine]
ATP + [SAMP2]-Gly-Gly + [UbaA]-L-cysteine
AMP + diphosphate + N6-[[SAMP2]-Gly-Gly]-[[UbaA]-L-cysteine]
ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine]
ATP + [SAMP3]-Gly-Gly + [UbaA]-L-cysteine
AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[UbaA]-L-cysteine]
ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine]
-
-
-
?
ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine]
the enzyme is required for the formation of both SAMP1- and SAMP2-protein conjugates
-
-
?
ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine]
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
-
-
?
ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine]
the enzyme is required for the formation of both SAMP1- and SAMP2-protein conjugates
-
-
?
ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine]
Haloferax volcanii YW1001
-
-
-
-
?
ATP + [SAMP1]-Gly-Gly + [UbaA]-L-cysteine
AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[UbaA]-L-cysteine]
-
-
-
?
ATP + [SAMP1]-Gly-Gly + [UbaA]-L-cysteine
AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[UbaA]-L-cysteine]
-
-
-
-
?
ATP + [SAMP1]-Gly-Gly + [UbaA]-L-cysteine
AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[UbaA]-L-cysteine]
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
-
-
?
ATP + [SAMP1]-Gly-Gly + [UbaA]-L-cysteine
AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[UbaA]-L-cysteine]
Haloferax volcanii YW1001
-
-
-
-
?
ATP + [SAMP2]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP2]-Gly-Gly]-[[protein]-L-lysine]
the enzyme is required for the formation of both SAMP1- and SAMP2-protein conjugates
-
-
?
ATP + [SAMP2]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP2]-Gly-Gly]-[[protein]-L-lysine]
the enzyme is required for the formation of both SAMP1- and SAMP2-protein conjugates
-
-
?
ATP + [SAMP2]-Gly-Gly + [UbaA]-L-cysteine
AMP + diphosphate + N6-[[SAMP2]-Gly-Gly]-[[UbaA]-L-cysteine]
-
-
-
?
ATP + [SAMP2]-Gly-Gly + [UbaA]-L-cysteine
AMP + diphosphate + N6-[[SAMP2]-Gly-Gly]-[[UbaA]-L-cysteine]
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
-
-
?
ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine]
-
-
-
?
ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine]
-
-
-
r
ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[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
-
-
?
ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine]
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
-
-
r
ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine]
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
-
-
?
ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[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
-
-
?
ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine
AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine]
Haloferax volcanii YW1001
-
-
-
-
?
ATP + [SAMP3]-Gly-Gly + [UbaA]-L-cysteine
AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[UbaA]-L-cysteine]
-
-
-
?
ATP + [SAMP3]-Gly-Gly + [UbaA]-L-cysteine
AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[UbaA]-L-cysteine]
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
-
-
?
additional information
?
-
many of the sampylated proteins that are identified (from cells grown aerobically on DMSO) are homologues of sulfur metabolism, oxidative stress, and/or autoregulation. Proteins found multiply modified by sampylation are examples of this association including the E1-like UbaA, the ubiquitin-like SAMP3 (related to SAMP1), the large subunit of MPT synthase (MoaE), and a methionine sulfoxide-S-reductase homologue (MsrA)
-
-
?
additional information
?
-
-
many of the sampylated proteins that are identified (from cells grown aerobically on DMSO) are homologues of sulfur metabolism, oxidative stress, and/or autoregulation. Proteins found multiply modified by sampylation are examples of this association including the E1-like UbaA, the ubiquitin-like SAMP3 (related to SAMP1), the large subunit of MPT synthase (MoaE), and a methionine sulfoxide-S-reductase homologue (MsrA)
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
many of the sampylated proteins that are identified (from cells grown aerobically on DMSO) are homologues of sulfur metabolism, oxidative stress, and/or autoregulation. Proteins found multiply modified by sampylation are examples of this association including the E1-like UbaA, the ubiquitin-like SAMP3 (related to SAMP1), the large subunit of MPT synthase (MoaE), and a methionine sulfoxide-S-reductase homologue (MsrA)
-
-
?
additional information
?
-
Haloferax volcanii YW1001
-
many of the sampylated proteins that are identified (from cells grown aerobically on DMSO) are homologues of sulfur metabolism, oxidative stress, and/or autoregulation. Proteins found multiply modified by sampylation are examples of this association including the E1-like UbaA, the ubiquitin-like SAMP3 (related to SAMP1), the large subunit of MPT synthase (MoaE), and a methionine sulfoxide-S-reductase homologue (MsrA)
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
ATP hydrolysis triggers the formation of thioester and peptide bonds within the Ubl:E1-like complex, docking of ATP
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
DMSO
levels of samp3ylated proteins and samp3 transcripts are increased by the addition of dimethyl sulfoxide to aerobically growing cells
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Brain Diseases
Biallelic UFM1 and UFC1 mutations expand the essential role of ufmylation in brain development.
Dehydration
A cyclic form of N6-threonylcarbamoyladenosine as a widely distributed tRNA hypermodification.
Microcephaly
Biallelic UFM1 and UFC1 mutations expand the essential role of ufmylation in brain development.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kinetics and thermodynamics of the enzyme with wild-type and mutant SAMP substrates, overview
-
additional information
additional information
-
kinetics and thermodynamics of the enzyme with wild-type and mutant SAMP substrates, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
SwissProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
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
evolution
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
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
-
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
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
-
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
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
physiological function
the archaeon Haloferax volcanii uses SAMP1 as a protein modifier to regulate and orchestrate cellular functions. SAMP1 is ligated to proteins by transfer via SAMP-activating E1 enzyme UbaA, i.e. samp1ylation. SAMP1 is a ubiquitin-like protein modifier that is relatively specific in tagging its protein partners as well as proteins associated with oxidative stress response. SAMP1 modifies a relatively small number of protein targets. SAMPs are activated (adenylated) in an ATP-dependent manner by the E1-like UbaA/ELSA and liberated from SAMP conjugates by the action of the JAMM/MPN+ Zn2+-metalloprotease HvJAMM1. SAMP1 conjugation is speculated to regulate the catalytic activity of MPT synthase, the conserved K240 and K247 residues of MoaE, the large subunit of MPT synthase, are found to be covalently attached to C-terminus of SAMP1
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
physiological function
Haloferax volcanii YW1001
-
the archaeon Haloferax volcanii uses SAMP1 as a protein modifier to regulate and orchestrate cellular functions. SAMP1 is ligated to proteins by transfer via SAMP-activating E1 enzyme UbaA, i.e. samp1ylation. SAMP1 is a ubiquitin-like protein modifier that is relatively specific in tagging its protein partners as well as proteins associated with oxidative stress response. SAMP1 modifies a relatively small number of protein targets. SAMPs are activated (adenylated) in an ATP-dependent manner by the E1-like UbaA/ELSA and liberated from SAMP conjugates by the action of the JAMM/MPN+ Zn2+-metalloprotease HvJAMM1. SAMP1 conjugation is speculated to regulate the catalytic activity of MPT synthase, the conserved K240 and K247 residues of MoaE, the large subunit of MPT synthase, are found to be covalently attached to C-terminus of SAMP1
-
physiological function
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
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
-
physiological function
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
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
-
physiological function
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
the archaeon Haloferax volcanii uses SAMP1 as a protein modifier to regulate and orchestrate cellular functions. SAMP1 is ligated to proteins by transfer via SAMP-activating E1 enzyme UbaA, i.e. samp1ylation. SAMP1 is a ubiquitin-like protein modifier that is relatively specific in tagging its protein partners as well as proteins associated with oxidative stress response. SAMP1 modifies a relatively small number of protein targets. SAMPs are activated (adenylated) in an ATP-dependent manner by the E1-like UbaA/ELSA and liberated from SAMP conjugates by the action of the JAMM/MPN+ Zn2+-metalloprotease HvJAMM1. SAMP1 conjugation is speculated to regulate the catalytic activity of MPT synthase, the conserved K240 and K247 residues of MoaE, the large subunit of MPT synthase, are found to be covalently attached to C-terminus of SAMP1
-
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
-
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
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
additional information
the crystal structure of SAMP1, PDB ID 3PO0, is docked to the three-dimensional model of UbaA using the Escherichia coli MoaD-MoeB complex as a template, PDB ID 1JW9. Enzyme UbaA dimeric complex structure modeling, and ab initio modeling of the remaining 25 residues of UbaA, which include the highly disordered N- and C-termini
additional information
-
the crystal structure of SAMP1, PDB ID 3PO0, is docked to the three-dimensional model of UbaA using the Escherichia coli MoaD-MoeB complex as a template, PDB ID 1JW9. Enzyme UbaA dimeric complex structure modeling, and ab initio modeling of the remaining 25 residues of UbaA, which include the highly disordered N- and C-termini
additional information
Haloferax volcanii YW1001
-
the crystal structure of SAMP1, PDB ID 3PO0, is docked to the three-dimensional model of UbaA using the Escherichia coli MoaD-MoeB complex as a template, PDB ID 1JW9. Enzyme UbaA dimeric complex structure modeling, and ab initio modeling of the remaining 25 residues of UbaA, which include the highly disordered N- and C-termini
-
additional information
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
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
-
additional information
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
the crystal structure of SAMP1, PDB ID 3PO0, is docked to the three-dimensional model of UbaA using the Escherichia coli MoaD-MoeB complex as a template, PDB ID 1JW9. Enzyme UbaA dimeric complex structure modeling, and ab initio modeling of the remaining 25 residues of UbaA, which include the highly disordered N- and C-termini
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). UBAA_HALVD
Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)
270
0
28704
Swiss-Prot
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
many of the sampylated proteins that are identified are homologues of sulfur metabolism, oxidative stress, and/or autoregulation. Proteins found multiply modified by sampylation are examples of this association including the E1-like UbaA, the ubiquitin-like SAMP3 (related to SAMP1), the large subunit of MPT synthase (MoaE), and a methionine sulfoxide-S-reductase homologue (MsrA)
additional information
-
many of the sampylated proteins that are identified are homologues of sulfur metabolism, oxidative stress, and/or autoregulation. Proteins found multiply modified by sampylation are examples of this association including the E1-like UbaA, the ubiquitin-like SAMP3 (related to SAMP1), the large subunit of MPT synthase (MoaE), and a methionine sulfoxide-S-reductase homologue (MsrA)
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
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
additional information
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
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
-
additional information
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
many of the sampylated proteins that are identified are homologues of sulfur metabolism, oxidative stress, and/or autoregulation. Proteins found multiply modified by sampylation are examples of this association including the E1-like UbaA, the ubiquitin-like SAMP3 (related to SAMP1), the large subunit of MPT synthase (MoaE), and a methionine sulfoxide-S-reductase homologue (MsrA)
-
additional information
Haloferax volcanii YW1001
-
many of the sampylated proteins that are identified are homologues of sulfur metabolism, oxidative stress, and/or autoregulation. Proteins found multiply modified by sampylation are examples of this association including the E1-like UbaA, the ubiquitin-like SAMP3 (related to SAMP1), the large subunit of MPT synthase (MoaE), and a methionine sulfoxide-S-reductase homologue (MsrA)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C188S
additional information
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
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
-
additional information
construction of a mutant strain HM1052, a DELTAubaA E1-like mutant
additional information
-
construction of a mutant strain HM1052, a DELTAubaA E1-like mutant
additional information
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
construction of a mutant strain HM1052, a DELTAubaA E1-like mutant
-
additional information
Haloferax volcanii YW1001
-
construction of a mutant strain HM1052, a DELTAubaA E1-like mutant
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Miranda, H.V.; Antelmann, H.; Hepowit, N.; Chavarria, N.E.; Krause, D.J.; Pritz, J.R.; Bsell, 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
Mol. Cell. Proteomics
13
220-239
2013
Haloferax volcanii (D4GSF3), Haloferax volcanii DSM 3757 (D4GSF3)
brenda
Humbard, M.A.; Miranda, H.V.; Lim, J.M.; Krause, D.J.; Pritz, J.R.; Zhou, G.; Chen, S.; Wells, L.; Maupin-Furlow, J.A.
Ubiquitin-like small archaeal modifier proteins (SAMPs) in Haloferax volcanii
Nature
463
54-60
2010
Haloferax volcanii (D4GSF3), Haloferax volcanii DSM 3757 (D4GSF3)
brenda
Chavarria, N.E.; Hwang, S.; Cao, S.; Fu, X.; Holman, M.; Elbanna, D.; Rodriguez, S.; Arrington, D.; Englert, M.; Uthandi, S.; Sll, D.; Maupin-Furlow, J.A.
Archaeal Tuc1/Ncs6 homolog required for wobble uridine tRNA thiolation is associated with ubiquitin-proteasome, translation, and RNA processing system homologs
PLoS One
9
e99104
2014
Haloferax volcanii (D4GSF3), Haloferax volcanii DSM 3757 (D4GSF3)
brenda
Miranda, H.V.; Nembhard, N.; Su, D.; Hepowit, N.; Krause, D.J.; Pritz, J.R.; Phillips, C.; Sll, D.; Maupin-Furlow, J.A.
E1- and ubiquitin-like proteins provide a direct link between protein conjugation and sulfur transfer in archaea
Proc. Natl. Acad. Sci. USA
108
4417-4422
2011
Haloferax volcanii (D4GSF3), Haloferax volcanii, Haloferax volcanii DSM 3757 (D4GSF3)
brenda
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
FEBS J.
183
3567-3586
2016
Haloferax volcanii (D4GSF3), Haloferax volcanii, Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2 (D4GSF3)
brenda
Miranda, H.; Antelmann, H.; Hepowit, N.; Chavarria, N.; Krause, D.; Pritz, J.; Bäsell, K.; Becher, D.; Humbard, M.; Brocchieri, L.; Maupin-Furlow, J.
Archaeal ubiquitin-like SAMP3 is isopeptide-linked to proteins via a UbaA-dependent mechanism
Mol. Cell. Proteomics
13
220-239
2014
Haloferax volcanii (D4GSF3), Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2 (D4GSF3)
brenda
Dantuluri, S.; Wu, Y.; Hepowit, N.L.; Chen, H.; Chen, S.; Maupin-Furlow, J.A.
Proteome targets of ubiquitin-like samp1ylation are associated with sulfur metabolism and oxidative stress in Haloferax volcanii
Proteomics
16
1100-1110
2016
Haloferax volcanii (D4GSF3), Haloferax volcanii, Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2 (D4GSF3)
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 6.2.1.55)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
