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Information on EC 6.1.1.7 - alanine-tRNA ligase and Organism(s) Pyrococcus horikoshii and UniProt Accession O58035

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Pyrococcus horikoshii
UNIPROT: O58035 not found.
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The taxonomic range for the selected organisms is: Pyrococcus horikoshii
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
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Alanine transfer RNA synthetase
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Alanine translase
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Alanine tRNA synthetase
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Alanine--tRNA ligase
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Alanine-transfer RNA ligase
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Alanyl-transfer ribonucleate synthetase
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Alanyl-transfer ribonucleic acid synthetase
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Alanyl-transfer RNA synthetase
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Alanyl-tRNA synthetase
AlaRS
Synthase, alanyl-transfer ribonucleate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
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Aminoacylation
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
L-alanine:tRNAAla ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9031-71-4
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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
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
active site bound by His9, His13, His120, and Cys116, involved in the catalytic reaction
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18152
1 * 18152, crystal structure analysis, two-domain structure consisting of seven antiparallel beta-sheets and six helices
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 18152, crystal structure analysis, two-domain structure consisting of seven antiparallel beta-sheets and six helices
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
monomer structures of C-terminally truncated AlaRS, with both activation and editing domains in the apo form, in complex with an Ala-AMP analog, and in a high-resolution lysine-methylated form. Docking of the editing domain to the activation domain occurs opposite from the predicted tRNA-binding surface. The editing site is positioned more than 35 A from the activation site. Results suggest that tRNA translocation via a canonical CCA flipping is unlikely to occur in AlaRS. Zinc binds in the editing site, in which the specific coordination of zinc will be facilitated by a conserved GGQ motif
purified recombinant wild-type and selenomethionine-labeld AlaRS editing-domain homolog, PH0574, 37.6 mg/ml protein, 27.5%w/v PEG 4000, and 100 mM MES-Na, pH 6.3, using a full-automatic protein crystallization and observation system, X-ray diffraction structure determination and analysis at 1.45 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant PH0574, from Escherichia coli strain BL21 by two steps of anion exchange chromatography, hydroxyapatite chromatography, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene PH0574, expression in Escherichia coli strain BL21
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ishijima, J.; Uchida, Y.; Kuroishi, C.; Tuzuki, C.; Takahashi, N.; Okazaki, N.; Yutani, K.; Miyano, M.
Crystal structure of alanyl-tRNA synthetase editing-domain homolog (PH0574) from a hyperthermophile, Pyrococcus horikoshii OT3 at 1.45 A resolution
Proteins
62
1133-1137
2006
Pyrococcus horikoshii (O58307), Pyrococcus horikoshii OT-3 (O58307)
Manually annotated by BRENDA team
Sokabe, M.; Ose, T.; Nakamura, A.; Tokunaga, K.; Nureki, O.; Yao, M.; Tanaka, I.
The structure of alanyl-tRNA synthetase with editing domain
Proc. Natl. Acad. Sci. USA
106
11028-11033
2009
Pyrococcus horikoshii (O58035)
Manually annotated by BRENDA team