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Information on EC 2.7.7.108 - protein adenylyltransferase
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2.7.7.108 protein adenylyltransferaseIUBMB Comments
The enzyme, commonly referred to as AMPylase, transfers an adenylyl (adenosine 5'-phosphate) group from ATP to L-serine, L-threonine, and L-tyrosine residues in its target protein substrates. AMPylation is found in both prokaryotes and eukaryotes. In bacteria AMPylases are abundant enzymes that either regulate the function of endogenous bacterial proteins or are translocated into host cells to hijack host cell signalling processes. Metazoans AMPylases are either enzymes containing a conserved Fic domain that primarily modify the ER-resident chaperone BiP, or mitochondrial selenocysteine-containing proteins (SelO) involved in redox signalling.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
+
a [protein]-L-serine
=
+
a [protein]-O-(5'-adenylyl)-L-serine
+
a [protein]-L-threonine
=
+
a [protein]-O-(5'-adenylyl)-L-threonine
+
=
+
a [protein]-O-(5'-adenylyl)-L-tyrosine
Synonyms
fic-1, pfhb2, ampylase, selenoo, fmp40, cg9523, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosine monophosphate-protein transferase
AMPylase
BepA
DrrA
Fic
FICD
FMP40
IbpA
SELENOO
-
-
-
-
selO
SidM
VbhT
VopS
AMPylase
-
-
-
-
DrrA
-
-
-
-
FICD
-
-
-
-
FMP40
-
-
-
-
IbpA
-
-
-
-
selO
-
-
-
-
VopS
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + a [protein]-L-serine = diphosphate + a [protein]-O-(5'-adenylyl)-L-serine
(1)
-
-
-
ATP + a [protein]-L-threonine = diphosphate + a [protein]-O-(5'-adenylyl)-L-threonine
(2)
-
-
-
ATP + a [protein]-L-tyrosine = diphosphate + a [protein]-O-(5'-adenylyl)-L-tyrosine
(3)
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
[protein] L-serine/L-threonine/L-tyrosine adenylyltransferase
The enzyme, commonly referred to as AMPylase, transfers an adenylyl (adenosine 5'-phosphate) group from ATP to L-serine, L-threonine, and L-tyrosine residues in its target protein substrates. AMPylation is found in both prokaryotes and eukaryotes. In bacteria AMPylases are abundant enzymes that either regulate the function of endogenous bacterial proteins or are translocated into host cells to hijack host cell signalling processes. Metazoans AMPylases are either enzymes containing a conserved Fic domain that primarily modify the ER-resident chaperone BiP, or mitochondrial selenocysteine-containing proteins (SelO) involved in redox signalling.
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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 + [Hsp-3]-L-threonine
diphosphate + [Hsp-3]-O-(5'-adenylyl)-L-threonine
Hsp-3 is AMPylated on Thr176
-
-
?
ATP + [HSP70 chaperone Grp78/BiP]-L-threonine
diphosphate + [HSP70 chaperone Grp78/BiP]-O-(5'-adenylyl)-L-threonine
the modified site is Thr366
-
-
?
ATP + [Rab1b]
diphosphate + [Rab1b]-AMP
-
-
catalyzes stable adenylylation of Rab1b, a regulator of endoplasmatic reticulum to Golgi trafficking, at residue Tyr77. Asp112 of DrrA functions as the catalytic base for deprotonation of Tyr77 of Rab1b to enable nucleophilic attack on the ATP
-
?
ATP + [Rho]-L-threonine
diphosphate + [Rho]-O-(5'-adenylyl)-L-threonine
modifies Thr35 in the switch I loop of small Rho GTPase
-
-
?
ATP + [Cdc42]-L-threonine
diphosphate + [Cdc42]-O-(5'-adenylyl)-L-threonine
-
-
-
?
ATP + [Cdc42]-L-threonine
diphosphate + [Cdc42]-O-(5'-adenylyl)-L-threonine
-
-
-
?
ATP + [CDC42]-L-tyrosine
diphosphate + [CDC42]-O-(5'-adenylyl)-L-tyrosine
-
-
-
?
ATP + [CDC42]-L-tyrosine
diphosphate + [CDC42]-O-(5'-adenylyl)-L-tyrosine
AMPylation occurs at the conserved tyrosine residue Tyr32 in the switch I region of the CDC42
-
-
?
ATP + [CDC42]-L-tyrosine
diphosphate + [CDC42]-O-(5'-adenylyl)-L-tyrosine
the reaction mechanisms probably follows a substrate-assisted attack of ATP. According to this model, His-3717 acts by attracting a proton from the Tyr substrate, thereby preparing the Tyr as a nucleophile to attack the alpha-phosphate of ATP
-
-
?
ATP + [CDC42]-L-tyrosine
diphosphate + [CDC42]-O-(5'-adenylyl)-L-tyrosine
the reaction mechanisms probably follows a substrate-assisted attack of ATP. According to this model, His-3717 acts by attracting a proton from the Tyr substrate, thereby preparing the Tyr as a nucleophile to attack the alpha-phosphate of ATP
-
-
?
ATP + [CDC42]-L-tyrosine
diphosphate + [CDC42]-O-(5'-adenylyl)-L-tyrosine
AMPylation occurs at the conserved tyrosine residue Tyr32 in the switch I region of the CDC42
-
-
?
ATP + [CDC42]-L-tyrosine
diphosphate + [CDC42]-O-(5'-adenylyl)-L-tyrosine
-
-
-
?
ATP + [pRab1]-L-tyrosine
diphosphate + [pRab1]-O-(5'-adenylyl)-L-tyrosine
AMPylates Rab1 on Tyr77
-
-
?
ATP + [pRab1]-L-tyrosine
diphosphate + [pRab1]-O-(5'-adenylyl)-L-tyrosine
AMPylates Rab1 on Tyr77, a conserved Tyr located in the switch II domain of the GTPase
-
-
?
ATP + [Rac1]-L-tyrosine
diphosphate + [Rac1]-O-(5'-adenylyl)-L-tyrosine
AMPylation occurs at the conserved tyrosine residue Tyr32 in the switch I region of the Rac1
-
-
?
ATP + [Rac1]-L-tyrosine
diphosphate + [Rac1]-O-(5'-adenylyl)-L-tyrosine
AMPylation occurs at the conserved tyrosine residue Tyr32 in the switch I region of the Rac1
-
-
?
ATP + [RhoA]-L-tyrosine
diphosphate + [RhoA]-O-(5'-adenylyl)-L-tyrosine
AMPylation occurs at the conserved tyrosine residue Tyr34 in the switch I region of the RhoA
-
-
?
ATP + [RhoA]-L-tyrosine
diphosphate + [RhoA]-O-(5'-adenylyl)-L-tyrosine
AMPylation occurs at the conserved tyrosine residue Tyr34 in the switch I region of the RhoA
-
-
?
additional information
?
-
a proteolysis resistant fragment (residues 10-302) that includes the Fic domain shows autoadenylylation activity
-
-
-
additional information
?
-
a proteolysis resistant fragment (residues 10-302) that includes the Fic domain shows autoadenylylation activity
-
-
-
additional information
?
-
AMPylation of human HSP40 and HSP70 as well as HSP-1 (in vitro) and Ssa2 (both in vitro and in vivo) is attributed to Fic-1 (E274G) activity
-
-
-
additional information
?
-
-
catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins. The enzyme prefers ATP over other nucleotides as a co-substrate
-
-
-
additional information
?
-
ctalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins
-
-
-
additional information
?
-
-
the enzyme transfers AMP to Rho, Rac1 and Cdc42
-
-
-
additional information
?
-
catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins
-
-
-
additional information
?
-
catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins
-
-
-
additional information
?
-
-
catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins
-
-
-
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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 + [Hsp-3]-L-threonine
diphosphate + [Hsp-3]-O-(5'-adenylyl)-L-threonine
Hsp-3 is AMPylated on Thr176
-
-
?
ATP + [HSP70 chaperone Grp78/BiP]-L-threonine
diphosphate + [HSP70 chaperone Grp78/BiP]-O-(5'-adenylyl)-L-threonine
the modified site is Thr366
-
-
?
ATP + [Rho]-L-threonine
diphosphate + [Rho]-O-(5'-adenylyl)-L-threonine
modifies Thr35 in the switch I loop of small Rho GTPase
-
-
?
ATP + [Cdc42]-L-threonine
diphosphate + [Cdc42]-O-(5'-adenylyl)-L-threonine
-
-
-
?
ATP + [Cdc42]-L-threonine
diphosphate + [Cdc42]-O-(5'-adenylyl)-L-threonine
-
-
-
?
ATP + [CDC42]-L-tyrosine
diphosphate + [CDC42]-O-(5'-adenylyl)-L-tyrosine
-
-
-
?
ATP + [CDC42]-L-tyrosine
diphosphate + [CDC42]-O-(5'-adenylyl)-L-tyrosine
AMPylation occurs at the conserved tyrosine residue Tyr32 in the switch I region of the CDC42
-
-
?
ATP + [CDC42]-L-tyrosine
diphosphate + [CDC42]-O-(5'-adenylyl)-L-tyrosine
AMPylation occurs at the conserved tyrosine residue Tyr32 in the switch I region of the CDC42
-
-
?
ATP + [CDC42]-L-tyrosine
diphosphate + [CDC42]-O-(5'-adenylyl)-L-tyrosine
-
-
-
?
ATP + [pRab1]-L-tyrosine
diphosphate + [pRab1]-O-(5'-adenylyl)-L-tyrosine
AMPylates Rab1 on Tyr77
-
-
?
ATP + [pRab1]-L-tyrosine
diphosphate + [pRab1]-O-(5'-adenylyl)-L-tyrosine
AMPylates Rab1 on Tyr77, a conserved Tyr located in the switch II domain of the GTPase
-
-
?
ATP + [Rac1]-L-tyrosine
diphosphate + [Rac1]-O-(5'-adenylyl)-L-tyrosine
AMPylation occurs at the conserved tyrosine residue Tyr32 in the switch I region of the Rac1
-
-
?
ATP + [Rac1]-L-tyrosine
diphosphate + [Rac1]-O-(5'-adenylyl)-L-tyrosine
AMPylation occurs at the conserved tyrosine residue Tyr32 in the switch I region of the Rac1
-
-
?
ATP + [RhoA]-L-tyrosine
diphosphate + [RhoA]-O-(5'-adenylyl)-L-tyrosine
AMPylation occurs at the conserved tyrosine residue Tyr34 in the switch I region of the RhoA
-
-
?
ATP + [RhoA]-L-tyrosine
diphosphate + [RhoA]-O-(5'-adenylyl)-L-tyrosine
AMPylation occurs at the conserved tyrosine residue Tyr34 in the switch I region of the RhoA
-
-
?
additional information
?
-
a proteolysis resistant fragment (residues 10-302) that includes the Fic domain shows autoadenylylation activity
-
-
-
additional information
?
-
a proteolysis resistant fragment (residues 10-302) that includes the Fic domain shows autoadenylylation activity
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
the enzyme AMPylates the endoplasmic reticulum-resident HSP70 chaperone Grp78/BiP in a Ca2+-dependent manner
Mg2+
maximal activity in the presence of Mn2+ or Mg2+. The active site-embedded residue Asp367 (HPFIDGNGR) coordinates a Mg2+ ion that bridges the alpha- and beta-phosphates of ATP during catalysis and is essential for catalysis
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the enzyme predominantly localizes to the ER-nuclear envelope continuum
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
-
the enzyme catalyzes the covalent transfer of AMP to proteins. This posttranslational modification regulates the function of several proteins, including the ER-resident chaperone Grp78/BiP
physiological function
evolution
-
SelO is one of the most highly conserved members of either the human protein kinase families or the various selenoprotein families. Among bacteria, SelO is ubiquitous in Proteobacteria and Cyanobacteria while in other phyla it is less frequent. Among eukaryotes, in most phyla there is on average one SelO gene per genome, while chordates and arthropods are exceptions, having an average of two or 0.14 genes per genome, respectively
evolution
-
SelO is one of the most highly conserved members of either the human protein kinase families or the various selenoprotein families. Among bacteria, SelO is ubiquitous in Proteobacteria and Cyanobacteria while in other phyla it is less frequent. Among eukaryotes, in most phyla there is on average one SelO gene per genome, while chordates and arthropods are exceptions, having an average of two or 0.14 genes per genome, respectively
evolution
SelO is one of the most highly conserved members of either the human protein kinase families or the various selenoprotein families. Among bacteria, SelO is ubiquitous in Proteobacteria and Cyanobacteria while in other phyla it is less frequent. Among eukaryotes, in most phyla there is on average one SelO gene per genome, while chordates and arthropods are exceptions, having an average of two or 0.14 genes per genome, respectively
evolution
SelO is one of the most highly conserved members of either the human protein kinase families or the various selenoprotein families. Among bacteria, SelO is ubiquitous in Proteobacteria and Cyanobacteria while in other phyla it is less frequent. Among eukaryotes, in most phyla there is on average one SelO gene per genome, while chordates and arthropods are exceptions, having an average of two or 0.14 genes per genome, respectively
evolution
the nucleotide-binding mechanism is conserved among Fic proteins
evolution
-
SelO is one of the most highly conserved members of either the human protein kinase families or the various selenoprotein families. Among bacteria, SelO is ubiquitous in Proteobacteria and Cyanobacteria while in other phyla it is less frequent. Among eukaryotes, in most phyla there is on average one SelO gene per genome, while chordates and arthropods are exceptions, having an average of two or 0.14 genes per genome, respectively
-
evolution
-
the nucleotide-binding mechanism is conserved among Fic proteins
-
malfunction
-
decrease in survival of SelO deficient cells with H2O2
malfunction
Fic-1 knock-out worms are more susceptible to infection by Pseudomonas aeruginosa
malfunction
HYPE knock-down prevents the induction of the ATF-6 and PERK-dependent UPRER branches
malfunction
knock-out flies are insensitive to light stimuli due to a failure to activate postsynaptic neurons
malfunction
-
mFICD deficiency is well tolerated in unstressed mice. mFICD-deficient mouse embryonic fibroblasts are depleted of AMPylated proteins. mFICD deletion alters protein synthesis and secretion in splenocytes, including that of IgM, an antibody secreted early during infections, and the proinflammatory cytokine IL-1beta, without affecting the unfolded protein response. Visual nonspatial shortterm learning is stronger in old mFICD-/- mice than in wild type controls while other measures of cognition, memory, and learning are unaffected
physiological function
AMPylation of Rab1b restricts binding of GTPase activating proteins (GAPs) and subsequent activation of Rab1b, thus locking Rab1b in the GTP-bound state. Simultaneously, AMPylation of Rab1b blocks downstream interactions with binding partners such as MICAL-3 and enhances retention of Rab1b at Legionella-containing vacuoles (LCVs) during infection
physiological function
cytotoxicity is mediated by disruption of cytoskeletal regulation, repression of immune signalling pathways downstream of Rho GTPases
physiological function
limited role for Fic-1 mediated AMPylation in the regulation of endoplasmic reticulum homeostasis
physiological function
protein AMPylation by Fic domain-containing proteins (Fic proteins) is an ancient and conserved post-translational modification. The enzyme covalently modifies heat-shock 70 family proteins, translation elongation factors and histones. FIC-1 modulates antimicrobial defense responses of Caenorhabditis elegans against Pseudomonas aeruginosa
physiological function
protein AMPylation, the covalent attachment of an adenosine 5'-monophosphate (AMP) residue to amino acid side chains using ATP as the donor, is a post-translational modification that is relevant for both normal and pathological cell signaling. In metazoans, single copies of fic-domain-containing AMPylases, the enzymes responsible for AMPylation, preferentially modify a set of dedicated targets and contribute to the perception of cellular stress and its regulation. Pathogenic bacteria can exploit AMPylation of eukaryotic target proteins to rewire host cell signaling machinery in support of their propagation and survival
physiological function
-
SelO-mediated AMPylation of proteins protects Saccharomyces cerevisiae from oxidative stress
physiological function
the enzyme (IbpA) from the bacterial pathogen Histophilus somni contains two Fic domains that adenylylate the switch1 Tyr residue of Rho-family GTPases, allowing the bacteria to subvert host defenses
physiological function
the enzyme disrupts host intracellular vesicle transport and evades capture by lysosomes
physiological function
-
the enzyme is involved in adaptive immunity and neuronal plasticity
physiological function
VopS-mediated AMPylation of Rho, Rac1 and Cdc42 impairs cellular signaling in several ways. The AMP moiety interferes with the binding of direct interaction partners, and also prevents E3 ubiquitin ligases from targeting these now non-functional AMPylated GTPases for proteolytic degradation. VopS also alters cellular immunity through inhibition of the pro-inflammatory NFkappaB signaling cascade, limits the generation of superoxide and attenuates Erk and JNK signaling. AMPylation of Rho GTPases further activates the pyrin-dependent inflammasome while inhibiting NLRC4-dependent inflammasome activation. As a direct consequence, the actin cytoskeleton collapses and cells rapidly die
physiological function
-
the enzyme (IbpA) from the bacterial pathogen Histophilus somni contains two Fic domains that adenylylate the switch1 Tyr residue of Rho-family GTPases, allowing the bacteria to subvert host defenses
-
physiological function
-
cytotoxicity is mediated by disruption of cytoskeletal regulation, repression of immune signalling pathways downstream of Rho GTPases
-
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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). VBHT_BARSR
Bartonella schoenbuchensis (strain DSM 13525 / NCTC 13165 / R1)
478
0
55379
Swiss-Prot
-
DRRA_LEGPN
647
0
73422
Swiss-Prot
other Location (Reliability: 1)
BEPA_BARHE
Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
544
0
61341
Swiss-Prot
-
VOPS_VIBPA
Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
387
0
41737
Swiss-Prot
-
SELO_PSESM
Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000)
487
0
55208
Swiss-Prot
other Location (Reliability: 5)
SOFIC_SHEON
Shewanella oneidensis (strain MR-1)
372
0
42225
Swiss-Prot
other Location (Reliability: 2)
SELO_HUMAN
669
0
73489
Swiss-Prot
Mitochondrion (Reliability: 4)
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
FIC-1 crystallizes as a dimer. The dimer is held together by two discrete interfaces that together bury 676.4 A of solvent-accessible surface area
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
the enzyme is proteolytically processed
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of a proteolysis resistant fragment (residues 10-302) that includes the Fic domain is determined to 2.9 A resolution by the SeMet-SAD method
the ATP substrate binds to the wild-type FIC domains, but with the alpha-phosphate in disparate and non-competent orientations. In E-G mutants, where the inhibitory glutamate residue is replaced by glycine, the triphosphate moiety is reorganized to the same tightly bound structure through a unique set of hydrogen bonds with Fic signature motif residues. The gamma-phosphate adopts the location that is taken by the inhibitory glutamate in wild-type resulting in an alpha-phosphate orientation that can be attacked in-line by a target side-chain hydroxyl group
crystals are obtained via hanging drop vapor diffusion and grew over two weeks at 18°C in 0.1 MMES pH 6.5 and 1.1 M ammonium sulfate using a 1:1 drop ratio with mother liquorcrystal structure of FIC-1 and its constitutively active mutant form FIC-1 E274G
crystals are grown at 4°C via sitting-drop vapor diffusion method. Structure of the second Fic domain of IbpA (IbpAFic2) in complex with its substrate
the ATP substrate binds to the wild-type FIC domains, but with the alpha-phosphate in disparate and non-competent orientations. In E-G mutants, where the inhibitory glutamate residue is replaced by glycine, the triphosphate moiety is reorganized to the same tightly bound structure through a unique set of hydrogen bonds with Fic signature motif residues. The gamma-phosphate adopts the location that is taken by the inhibitory glutamate in wild-type resulting in an alpha-phosphate orientation that can be attacked in-line by a target side-chain hydroxyl group
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E234G
HYPE E234G-medatied AMPylation of HSP-1 T342A is reduced as compared to wild type HSP-1
E274G
E274G/I298D
the mutant protein behaves as a monomer in solution
H404A
the mutant enzyme does not show detectable self-AMPylation. The mutant enzyme H404A does nor AMPylate histone H3
I298D
the mutant protein behaves as a monomer in solution. Relative to the capacity of mutant enzyme E274G to AMPylate histone H3, mutant enzyme E274G/I298D self-AMPylation is reduced to 46% and target AMPylation activity to 11%
G3724E
the mutant enzyme fails to adenylylate any of the Rho-family proteins in vitro, also completely lost its cell-rounding activity in vivo
H3717A
I3535E/P3536E
I3552E/L3553E
mutant displays impaired activity towards the Rho-family proteins. Approximately 50% of the cells expressing I3552E/L3553E remain morphologically normal
L3668A/K3670A
approximately 50% of the cells expressing L3668A/K3670A remain morphologically normal
R3728A/Q3757A
approximately 20% of the cells expressing R3728A/Q3757A remain morphologically normal
H3717A
I3535E/P3536E
I3552E/L3553E
-
mutant displays impaired activity towards the Rho-family proteins. Approximately 50% of the cells expressing I3552E/L3553E remain morphologically normal
-
E274G
animals that express the constitutively active Fic (E274G) mutant show enhanced tolerance to the Pseudomonas aeruginosa
E274G
the mutant enzyme exhibits a massive increase in self-modification as compared to wild-type enzyme. Mutant E274G is more promiscuous in its preference for nucleoside triphosphates than mutant E234G. The mutant enzyme E274G AMPylates histones H2A, H2B, H3.1, H3.2 H3.3 but not H1 or H4H3
H3717A
mutation of the conserved histidine residue (H3717A) in the IbpA Fic motif does not result in cytotoxicity
I3535E/P3536E
mutant displays impaired activity towards the Rho-family proteins
I3535E/P3536E
mutant is still capable of inducing pronounced cell rounding
H3717A
-
mutation of the conserved histidine residue (H3717A) in the IbpA Fic motif does not result in cytotoxicity
-
I3535E/P3536E
-
mutant displays impaired activity towards the Rho-family proteins
-
I3535E/P3536E
-
mutant is still capable of inducing pronounced cell rounding
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
an N-terminal His6-tagged construct of full-length BepA (64 kDa) is expressed in Escherichia coli BL21 (DE3)
expression in Rosetta DE3 cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
increase in SelO protein levels in cells grown on the non-fermentable carbon sources glycerol, lactate and acetate
-
presence of fic-1 mRNA throughout the body of the animal, including the germline, and at all developmental stages. Embryonic expression levels appeared comparatively high
the enzyme is expressed at low levels throughout the worm body, but is most pronounced in the adult germline and in embryonic cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gavriljuk, K.; Schartner, J.; Itzen, A.; Goody, R.S.; Gerwert, K.; Koetting, C.
Reaction mechanism of adenylyltransferase DrrA from Legionella pneumophila elucidated by time-resolved fourier transform infrared spectroscopy
J. Am. Chem. Soc.
136
9338-9345
2014
Legionella pneumophila
brenda
Goepfert, A.; Stanger, F.V.; Dehio, C.; Schirmer, T.
Conserved inhibitory mechanism and competent ATP binding mode for adenylyltransferases with Fic fold
PLoS ONE
8
e64901
2013
Bartonella schoenbuchensis (E6Z0R3), Shewanella oneidensis (Q8E9K5), Shewanella oneidensis MR-1 / ATCC 700550 (Q8E9K5), Bartonella schoenbuchensis DSM 13525 (E6Z0R3)
brenda
Sreelatha, A.; Yee, S.; Lopez, V.; Park, B.; Kinch, L.; Pilch, S.; Servage, K.; Zhang, J.; Jiou, J.; Karasiewicz-Urbanska, M.; Lobocka, M.; Grishin, N.; Orth, K.; Kucharczyk, R.; Pawlowski, K.; Tomchick, D.; Tagliabracci, V.
Protein AMPylation by an evolutionarily conserved pseudokinase
Cell
175
809-821.e19
2018
Saccharomyces cerevisiae, Escherichia coli, Pseudomonas syringae pv. tomato (Q87VB1), Homo sapiens (Q9BVL4), Pseudomonas syringae pv. tomato DC3000 (Q87VB1)
brenda
McCaul, N.; Porter, C.M.; Becker, A.; Tang, C.A.; Wijne, C.; Chatterjee, B.; Bousbaine, D.; Bilate, A.; Hu, C.A.; Ploegh, H.; Truttmann, M.C.
Deletion of mFICD AMPylase alters cytokine secretion and affects visual short-term learning invivo
J. Biol. Chem.
297
100991
2021
Mus musculus
brenda
Xiao, J.; Worby, C.; Mattoo, S.; Sankaran, B.; Dixon, J.
Structural basis of Fic-mediated adenylylation
Nat. Struct. Mol. Biol.
17
1004-1010
2010
Histophilus somni (Q06277), Histophilus somni 2336 (Q06277)
brenda
Chatterjee, B.; Truttmann, M.
Fic and non-Fic AMPylases Protein AMPylation in metazoans
Open Biology
11
210009
2021
Bartonella schoenbuchensis (E6Z0R3), Histophilus somni (Q06277), Legionella pneumophila (Q29ST3), Homo sapiens (Q9BVA6), Histophilus somni 2336 (Q06277), Bartonella schoenbuchensis DSM 13525 (E6Z0R3)
brenda
Truttmann, M.C.; Cruz, V.E.; Guo, X.; Engert, C.; Schwartz, T.U.; Ploegh, H.L.
The Caenorhabditis elegans protein FIC-1 is an AMPylase that covalently modifies heat-shock 70 family proteins, translation elongation factors and histones
PLoS Genet.
12
e1006023
2016
Caenorhabditis elegans (Q23544), Caenorhabditis elegans
brenda
Palanivelu, D.; Goepfert, A.; Meury, M.; Guye, P.; Dehio, C.; Schirmer, T.
Fic domain-catalyzed adenylylation Insight provided by the structural analysis of the type IV secretion system effector BepA
Protein Sci.
20
492-499
2011
Bartonella henselae (Q6G2A9), Bartonella henselae ATCC 49882 (Q6G2A9)
brenda
Truttmann, M.; Ploegh, H.
rAMPing up stress signaling Protein AMPylation in Metazoans
Trends Cell Biol.
27
608-620
2017
Pasteurella multocida, Histophilus somni (Q06277), Caenorhabditis elegans (Q23544), Legionella pneumophila (Q29ST3), Vibrio parahaemolyticus (Q87P32), Drosophila melanogaster (Q8SWV6), Histophilus somni 2336 (Q06277)
brenda
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