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Information on EC 6.1.1.9 - valine-tRNA ligase and Organism(s) Arabidopsis thaliana and UniProt Accession P93736

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This record set is specific for:
Arabidopsis thaliana
UNIPROT: P93736 not found.
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
Synonyms
valyl-trna synthetase, valrs, glp-4, val-trna synthetase, valyl-transfer rna synthetase, osvalrs2, valine-trna ligase, valyl-trna ligase, valyl transfer ribonucleic acid synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Valyl-tRNA synthetase
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G7a
-
-
-
-
Synthetase, valyl-transfer ribonucleate
-
-
-
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Valine transfer ribonucleate ligase
-
-
-
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Valine translase
-
-
-
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Valine--tRNA ligase
-
-
-
-
ValRS
-
-
-
-
Valyl transfer ribonucleic acid synthetase
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-
-
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Valyl-transfer ribonucleate synthetase
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-
-
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Valyl-transfer RNA synthetase
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-
-
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Valyl-tRNA ligase
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-
-
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Valyl-tRNA synthetase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
-
-
-
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Aminoacylation
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-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
L-valine:tRNAVal ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9023-47-6
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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
additional information
?
-
functional and evolutionary aspects of basic faced alpha helices, structural elements of aminoacyl-tRNA synthetases, overview
-
-
?
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
additional information
?
-
functional and evolutionary aspects of basic faced alpha helices, structural elements of aminoacyl-tRNA synthetases, overview
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cytoplasmic valRS
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SYVM1_ARATH
1108
0
125926
Swiss-Prot
Mitochondrion (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the enzyme possesses N terminal alpha-helices with basic residues distributed asymmetrically, on a single face of the helix, termed basic faced alpha helices, BFAHs, which are unique to the aminoacyl-tRNA synthetases, structural analysis, determination of distribution of basic residues within protein secondary structure by Fourier analysis, functional and evolutionary aspects of these structural features, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Massey, S.E.
Basic faced alpha-helices are widespread in the peptide extensions of the eukaryotic aminoacyl-tRNA synthetases
In Silico Biol.
6
259-273
2006
Saccharomyces cerevisiae, Homo sapiens (P26640), Takifugu rubripes (P49696), Arabidopsis thaliana (P93736), Oryza sativa (Q851K9)
Manually annotated by BRENDA team