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Literature summary extracted from

  • Chatterjee, B.; Truttmann, M.
    Fic and non-Fic AMPylases Protein AMPylation in metazoans (2021), Open Biology, 11, 210009 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.108 H348A AMPylation-deficient mutant Homo sapiens
2.7.7.108 H3717A mutation of the conserved histidine residue (H3717A) in the IbpA Fic motif does not result in cytotoxicity Histophilus somni

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.7.108 endoplasmic reticulum
-
Homo sapiens 5783
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.108 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 Homo sapiens
2.7.7.108 Mn2+ maximal activity in the presence of Mn2+ or Mg2+ Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.108 ATP + [CDC42]-L-tyrosine Histophilus somni AMPylation occurs at the conserved tyrosine residue Tyr32 in the switch I region of the CDC42 diphosphate + [CDC42]-O-(5'-adenylyl)-L-tyrosine
-
?
2.7.7.108 ATP + [CDC42]-L-tyrosine Histophilus somni 2336 AMPylation occurs at the conserved tyrosine residue Tyr32 in the switch I region of the CDC42 diphosphate + [CDC42]-O-(5'-adenylyl)-L-tyrosine
-
?
2.7.7.108 ATP + [pRab1]-L-tyrosine Legionella pneumophila AMPylates Rab1 on Tyr77, a conserved Tyr located in the switch II domain of the GTPase diphosphate + [pRab1]-O-(5'-adenylyl)-L-tyrosine
-
?
2.7.7.108 ATP + [Rac1]-L-tyrosine Histophilus somni AMPylation occurs at the conserved tyrosine residue Tyr32 in the switch I region of the Rac1 diphosphate + [Rac1]-O-(5'-adenylyl)-L-tyrosine
-
?
2.7.7.108 ATP + [Rac1]-L-tyrosine Histophilus somni 2336 AMPylation occurs at the conserved tyrosine residue Tyr32 in the switch I region of the Rac1 diphosphate + [Rac1]-O-(5'-adenylyl)-L-tyrosine
-
?
2.7.7.108 ATP + [RhoA]-L-tyrosine Histophilus somni AMPylation occurs at the conserved tyrosine residue Tyr34 in the switch I region of the RhoA diphosphate + [RhoA]-O-(5'-adenylyl)-L-tyrosine
-
?
2.7.7.108 ATP + [RhoA]-L-tyrosine Histophilus somni 2336 AMPylation occurs at the conserved tyrosine residue Tyr34 in the switch I region of the RhoA diphosphate + [RhoA]-O-(5'-adenylyl)-L-tyrosine
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.108 Bartonella schoenbuchensis E6Z0R3
-
-
2.7.7.108 Bartonella schoenbuchensis DSM 13525 E6Z0R3
-
-
2.7.7.108 Histophilus somni Q06277
-
-
2.7.7.108 Histophilus somni 2336 Q06277
-
-
2.7.7.108 Homo sapiens Q9BVA6
-
-
2.7.7.108 Legionella pneumophila Q29ST3
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.7.108 glycoprotein N-glycosylated at Asn275 Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.108 ATP + [CDC42]-L-tyrosine AMPylation occurs at the conserved tyrosine residue Tyr32 in the switch I region of the CDC42 Histophilus somni diphosphate + [CDC42]-O-(5'-adenylyl)-L-tyrosine
-
?
2.7.7.108 ATP + [CDC42]-L-tyrosine AMPylation occurs at the conserved tyrosine residue Tyr32 in the switch I region of the CDC42 Histophilus somni 2336 diphosphate + [CDC42]-O-(5'-adenylyl)-L-tyrosine
-
?
2.7.7.108 ATP + [pRab1]-L-tyrosine AMPylates Rab1 on Tyr77, a conserved Tyr located in the switch II domain of the GTPase Legionella pneumophila diphosphate + [pRab1]-O-(5'-adenylyl)-L-tyrosine
-
?
2.7.7.108 ATP + [Rac1]-L-tyrosine AMPylation occurs at the conserved tyrosine residue Tyr32 in the switch I region of the Rac1 Histophilus somni diphosphate + [Rac1]-O-(5'-adenylyl)-L-tyrosine
-
?
2.7.7.108 ATP + [Rac1]-L-tyrosine AMPylation occurs at the conserved tyrosine residue Tyr32 in the switch I region of the Rac1 Histophilus somni 2336 diphosphate + [Rac1]-O-(5'-adenylyl)-L-tyrosine
-
?
2.7.7.108 ATP + [RhoA]-L-tyrosine AMPylation occurs at the conserved tyrosine residue Tyr34 in the switch I region of the RhoA Histophilus somni diphosphate + [RhoA]-O-(5'-adenylyl)-L-tyrosine
-
?
2.7.7.108 ATP + [RhoA]-L-tyrosine AMPylation occurs at the conserved tyrosine residue Tyr34 in the switch I region of the RhoA Histophilus somni 2336 diphosphate + [RhoA]-O-(5'-adenylyl)-L-tyrosine
-
?

Subunits

EC Number Subunits Comment Organism
2.7.7.108 dimer
-
Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
2.7.7.108 DrrA
-
Legionella pneumophila
2.7.7.108 FICD
-
Homo sapiens
2.7.7.108 HypE
-
Homo sapiens
2.7.7.108 IbpA
-
Histophilus somni
2.7.7.108 SidM
-
Legionella pneumophila
2.7.7.108 VbhT
-
Bartonella schoenbuchensis

Expression

EC Number Organism Comment Expression
2.7.7.108 Homo sapiens endoplasmic reticulum stress elevates intracellular HYPE levels up

General Information

EC Number General Information Comment Organism
2.7.7.108 malfunction HYPE knock-down prevents the induction of the ATF-6 and PERK-dependent UPRER branches Homo sapiens
2.7.7.108 physiological function cytotoxicity is mediated by disruption of cytoskeletal regulation, repression of immune signalling pathways downstream of Rho GTPases Histophilus somni
2.7.7.108 physiological function the enzyme disrupts host intracellular vesicle transport and evades capture by lysosomes Legionella pneumophila