Information on EC 2.7.7.B4 - adenylyltransferase UBA4

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The expected taxonomic range for this enzyme is: Saccharomyces cerevisiae

EC NUMBER
COMMENTARY hide
2.7.7.B4
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
adenylyltransferase UBA4
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + Urm1p-terminal-Gly = diphosphate + Urm1p-terminal-Gly-AMP
show the reaction diagram
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + human MOCS2A-terminal-Gly
diphosphate + Urm1p-terminal-Gly-AMP
show the reaction diagram
the N-terminal domain of Uba4 catalyzes the activation of either MOCS2A (protein essential for the biosynthesis of the molybdenum cofactor in human) or Urm1 by formation of an acyl-adenylate bond. After adenylation, persulfurated Uba4 is able to form a thiocarboxylate group at the C-terminal glycine of either Urm1 or MOCS2A. The formation of a thioester intermediate between Uba4 and Urm1 or MOCS2A is not observed. The functional similarities between Uba4 and MOCS3 further demonstrate the evolutionary link between ATP-dependent protein conjugation and ATP-dependent cofactor sulfuration
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ATP + Urm1p-terminal-Gly
diphosphate + Urm1p-terminal-Gly-AMP
show the reaction diagram
Urm1p-terminal-Gly-AMP + Uba4-SSH
Urm1p-terminal-Gly-COSH + human MOCS2A-SH + AMP
show the reaction diagram
the N-terminal domain of Uba4 catalyzes the activation of Urm1 by formation of an acyl-adenylate bond. After adenylation, persulfurated Uba4 is able to form a thiocarboxylate group at the C-terminal glycine of Urm1. The formation of a thioester intermediate between Uba4 and Urm1 is not observed. The functional similarities between Uba4 and MOCS3 (protein essential for the biosynthesis of the molybdenum cofactor in human) further demonstrate the evolutionary link between ATP-dependent protein conjugation and ATP-dependent cofactor sulfuration
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + Urm1p-terminal-Gly
diphosphate + Urm1p-terminal-Gly-AMP
show the reaction diagram
Urm1p-terminal-Gly-AMP + Uba4-SSH
Urm1p-terminal-Gly-COSH + human MOCS2A-SH + AMP
show the reaction diagram
P38820
the N-terminal domain of Uba4 catalyzes the activation of Urm1 by formation of an acyl-adenylate bond. After adenylation, persulfurated Uba4 is able to form a thiocarboxylate group at the C-terminal glycine of Urm1. The formation of a thioester intermediate between Uba4 and Urm1 is not observed. The functional similarities between Uba4 and MOCS3 (protein essential for the biosynthesis of the molybdenum cofactor in human) further demonstrate the evolutionary link between ATP-dependent protein conjugation and ATP-dependent cofactor sulfuration
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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domain structure of Uba4p, consists of an amino N-terminal nucleotide-binding domain (NBD), followed by a MoeZ motif and a carboxy C-terminal rhodanese domain (RHD). Urm1p, adenylated by the nucleotide-binding domain (NBD) of Uba4p, is converted to a Urm1p-thiocarboxylate by Uba4p rhodanese domain (RHD). The sulfur is then passed onto U34 either directly or with the help of Ncs6p/Ncs2p
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purification of Uba and copurification of stable heterotetrameric complexes of Uba4 with both human Urm1 and MOCS2A
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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His-tagged Uba4p is recombinantly expressed in Escherichia coli strain Rosetta(DE3). The expression of the recombinant protein is induced by 2% lactose
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