Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 6.1.1.7 - alanine-tRNA ligase and Organism(s) Archaeoglobus fulgidus and UniProt Accession O28029

for references in articles please use BRENDA:EC6.1.1.7
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Archaeoglobus fulgidus
UNIPROT: O28029 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Archaeoglobus fulgidus
The enzyme appears in selected viruses and cellular organisms
Synonyms
alanyl-trna synthetase, alars, aars2, alanine trna synthetase, ala-trna synthetase, mitochondrial alanyl-trna synthetase, alanyl-transfer rna synthetase, mtalars, alanine-trna ligase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ala-tRNA synthetase
-
-
-
-
Alanine transfer RNA synthetase
-
-
-
-
Alanine translase
-
-
-
-
Alanine tRNA synthetase
-
-
-
-
Alanine--tRNA ligase
-
-
-
-
Alanine-transfer RNA ligase
-
-
-
-
Alanyl-transfer ribonucleate synthetase
-
-
-
-
Alanyl-transfer ribonucleic acid synthetase
-
-
-
-
Alanyl-transfer RNA synthetase
-
-
-
-
Alanyl-tRNA synthetase
AlaRS
Synthase, alanyl-transfer ribonucleate
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
-
-
-
-
Aminoacylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
L-alanine:tRNAAla ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9031-71-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-alanine + tRNAAla
AMP + diphosphate + L-alanyl-tRNAAla
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
AlaRS consists of four parts: an N-terminal aminoacylation active-site domain, a tRNA-recognition module, an editing domain and a C-terminal oligomerization domain
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
AlaRS-DELTAC, comprising the aminoacylation, tRNA-recognition, and editing domains, and AlaRS-C, comprising the dimerization domain. The aminoacylation/tRNA-recognition domains contain an insertion incompatible with the class-specific tRNA-binding mode. The editing domain is fixed tightly via hydrophobic interactions to the aminoacylation/tRNA-recognition domains, on the side opposite from that in threonyl-tRNA synthetase. A groove formed between the aminoacylation/tRNA-recognition domains and the editing domain appears to be an alternative tRNA-binding site. The amino acid residues required for the G3:U70 base pair recognition are mapped in this groove. The dimerization domain consists of helical and globular subdomains. The helical subdomain mediates dimerization by forming a helix–loop–helix zipper. The globular subdomain, which is important for the aminoacylation and editing activities, has a positively-charged face suitable for tRNA binding
purified recombinant full-length enzyme, N-terminal domain, and C-terminal domain, hanging-drop vapour-diffusion method, mixing of 0.001 ml of protein and reservoir solution, and equilibration against 0.5 ml of reservoir solution at 20°C, for crystallization of the AlaRS-FL–tRNAAla complex, tRNAAla is heated at 80°C for 5 min and is gradually cooled to room temperature for refolding, in presence of 1 mM AMP-PNP, different methods for the different protein samples are used, overview, X-ray diffraction structure determination and analysis at 3.2-3.5 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant full-length AlaRS and AlaRS domains from Escherichia coli strain BL21 by anion exchange chromatography followed by hydrophobic interaction and adsorption chromatography, respectively
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the full-length AlaRS, of the N-terminal fragment lacking the C-terminal oligomerization domain, residues 1-739, and of the C-terminal oligomerization domain of AlaRS, residues 737-906, in Escherichia coli strain BL21
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fukunaga, R.; Yokoyama, S.
Crystallization and preliminary X-ray crystallographic study of alanyl-tRNA synthetase from the archaeon Archaeoglobus fulgidus
Acta Crystallogr. Sect. F
63
224-228
2007
Archaeoglobus fulgidus
Manually annotated by BRENDA team
Naganuma, M.; Sekine, S.; Fukunaga, R.; Yokoyama, S.
Unique protein architecture of alanyl-tRNA synthetase for aminoacylation, editing, and dimerization
Proc. Natl. Acad. Sci. USA
106
8489-8494
2009
Archaeoglobus fulgidus (O28029), Archaeoglobus fulgidus
Manually annotated by BRENDA team