Literature summary for 6.2.1.45 extracted from

Bacik, J.P.; Walker, J.R.; Ali, M.; Schimmer, A.D.; Dhe-Paganon, S.
Crystal structure of the human ubiquitin-activating enzyme 5 (UBA5) bound to ATP: mechanistic insights into a minimalistic E1 enzyme (2010), J. Biol. Chem., 285, 20273-20280.

Cloned(Commentary)

Cloned (Comment)	Organism
-	Homo sapiens
expression in BL-21 cell	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
enzyme exists in two splice variants. To obtain high resolution crystals of UBA5, the N-terminal region of the long isoform, residues 156, are deleted and residues 330404 of the C-terminal domain are also removed. The removal of the CTD thus does not abrogate formation of the UBA5-UFM1 thioester intermediate. Crystals to 2.0 A resolution, and molecular replacement based on PDB structure 1ZFN. Structure shows similarities to both E1 and E1-like enzymes and is composed of an ATP-binding domain that consists of an eight-stranded beta-sheet surrounded by seven alpha-helices. UBA5 maintains a zinc-binding site that is coordinated by four cysteines with tetrahedral geometry	Homo sapiens
to 2.0 A resolution using molecular replacement based on PDB entry 1ZFN. UBA5 structure shows similarities to both E1 and E1-like enzymes and is composed of an ATP-binding domain that consists of an eight-stranded beta-sheet surrounded by seven alpha-helices. UBA5 maintains a zinc-binding site that is coordinated by four cysteines with tetrahedral geometry	Homo sapiens

Crystallization (Comment)

Organism

enzyme exists in two splice variants. To obtain high resolution crystals of UBA5, the N-terminal region of the long isoform, residues 156, are deleted and residues 330404 of the C-terminal domain are also removed. The removal of the CTD thus does not abrogate formation of the UBA5-UFM1 thioester intermediate. Crystals to 2.0 A resolution, and molecular replacement based on PDB structure 1ZFN. Structure shows similarities to both E1 and E1-like enzymes and is composed of an ATP-binding domain that consists of an eight-stranded beta-sheet surrounded by seven alpha-helices. UBA5 maintains a zinc-binding site that is coordinated by four cysteines with tetrahedral geometry

Homo sapiens

to 2.0 A resolution using molecular replacement based on PDB entry 1ZFN. UBA5 structure shows similarities to both E1 and E1-like enzymes and is composed of an ATP-binding domain that consists of an eight-stranded beta-sheet surrounded by seven alpha-helices. UBA5 maintains a zinc-binding site that is coordinated by four cysteines with tetrahedral geometry

Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
additional information	removal of residues 330-404 of the C-terminal domain does not abrogate formation of the UBA5-ubiquitin fold modifier1 thioester intermediate, the UBA5 C-terminal domain is not required for adenylation or thioester transfer of ubiquitin fold modifier1 to the UBA5 catalytic cysteine	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zinc	isoform UBA5 maintains a zinc-binding site that is coordinated by four cysteines with tetrahedral geometry	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9GZZ9	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + ubiquitin + [ubiquitin-activating enzyme Uba5]-L-cysteine	the catalytic cysteine residue of isoform Uba5 is part of the adenylation domain in a alpha-helical motif	Homo sapiens	AMP + diphosphate + [ubiquitin-activating enzyme Uba5]-S-ubiquitinyl-L-cysteine	-	?
ATP + ubiquitin fold modifier1 + [ubiquitin-activating enzyme Uba5]-L-cysteine	the catalytic cysteine residue of isoform Uba5 is part of the adenylation domain in a alpha-helical motif	Homo sapiens	AMP + diphosphate + [ubiquitin-activating enzyme Uba5]-S-(ubiquitin fold modifier1)-L-cysteine	-	?

Subunits

Subunits	Comment	Organism
dimer	analytical ultracentrifugation	Homo sapiens
dimer	analytical ultracentrifugation analysis, forms primarily dimers with 1.85:1 dimers to monomers ratio	Homo sapiens
monomer	analytical ultracentrifugation analysis, forms primarily dimers with 1.85:1 dimers to monomers ratio	Homo sapiens

Synonyms

Synonyms	Comment	Organism
UBA5	-	Homo sapiens
ubiquitin-activating enzyme 5	-	Homo sapiens
ubiquitin-like modifier-activating enzyme 5	-	Homo sapiens