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Information on EC 6.1.1.21 - histidine-tRNA ligase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P07263

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Saccharomyces cerevisiae
UNIPROT: P07263 not found.
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Synonyms
histidyl-trna synthetase, hisrs, hars2, jo-1 antigen, histidyl trna synthetase, histidyl-transfer rna synthetase, hars1, histidine-trna ligase, class ii histidyl-trna synthetase, mitochondrial histidyl trna synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Histidine translase
-
histidine-tRNA ligase
-
histidine-tRNA ligase homolog
-
Histidyl-transfer ribonucleate synthetase
-
Histidyl-tRNA synthetase
-
Synthetase, histidyl-transfer ribonucleate
-
HisRS
Histidine translase
Histidine--tRNA ligase
-
-
-
-
Histidine--tRNA ligase homolog
-
-
-
-
histidine-tRNA ligase
-
-
histidine-tRNA ligase homolog
-
-
Histidyl-transfer ribonucleate synthetase
histidyl-transfer RNA synthetase
-
-
Histidyl-tRNA synthetase
Jo-1 antigen
Synthetase, histidyl-transfer ribonucleate
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-histidine + tRNAHis = AMP + diphosphate + L-histidyl-tRNAHis
show the reaction diagram
N73 is a discriminator base involved in histidylation activity, substrate recognition mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
Aminoacylation
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
L-histidine:tRNAHis ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9068-78-4
-
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-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
show the reaction diagram
-
-
ir
ATP + L-histidine + minimalist RNA structures in a resected pseudoknot fold
AMP + diphosphate + L-histidyl-tRNAHis
show the reaction diagram
-
specifically recognized substrate, derived from tyrosine-accepting tRNA-like domain of brome mosaic virus RNA
-
?
ATP + L-histidine + RNA microhelix
?
show the reaction diagram
-
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidinyl-tRNAHis
show the reaction diagram
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
show the reaction diagram
ATP + L-histidine + tyrosine-accepting tRNA-like domain of brome mosaic virus RNA
AMP + diphosphate + L-histidyl-tyrosine-accepting tRNA-like domain of brome mosaic virus RNA
show the reaction diagram
-
specifically recognized substrate
-
?
additional information
?
-
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-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
show the reaction diagram
-
-
ir
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidinyl-tRNAHis
show the reaction diagram
-
-
-
-
?
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.14 - 0.5
ATP
0.0006 - 0.08
His
0.009
L-histidine
-
pH 8.0, 37°C, diphosphate exchange
0.124
RNA microhelix
-
pH 8.0, 37°C, aminoacylation
-
0.00014 - 0.00043
tRNAHis
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
40
ATP
-
pH 8.0, 37°C, diphosphate exchange
40
L-histidine
-
pH 8.0, 37°C, diphosphate exchange
0.0013
RNA microhelix
-
pH 8.0, 37°C, aminoacylation
-
0.417 - 0.42
tRNAHis
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1000
tRNAHis
-
pH 7.2, 37°C, wild-type substrate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
aminoacylation assay at
8
-
diphosphate exchange assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
aminoacylation assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
phylogenetic analysis reveals that tRNAThr1 originated from tRNAHis
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
x * 60000, amino acid sequence determination
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 60000, amino acid sequence determination
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
mutational study of the 1:73 base pair recognition by yeats HisRS using two chemically synthesized 24-nucleotide RNA microhelices, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
HTS1, phylogenetic analysis, expression in Escherichia coli strain BL21(DE3)
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rudinger, J.; Felden, B.; Florentz, C.; Giege, R.
Strategy for RNA recognition by yeast histidyl-tRNA synthetase
Bioorg. Med. Chem.
5
1001-1009
1997
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Boguslawski, G.; Vodkin, M.H.; Finkelstein, D.B.; Fink, G.R.
Histidyl-tRNAs and histidyl-tRNA synthetases in wild type and cytoplasmic petite mutants of Saccharomyces cerevisiae
Biochemistry
13
4659-4667
1974
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Freist, W.; Verhey, J.F.; Ruhlmann, A.; Gauss, D.H.; Arnez, J.G.
Histidyl-tRNA synthetase
Biol. Chem.
380
623-646
1999
Archaeoglobus fulgidus (O28631), Salmonella enterica subsp. enterica serovar Typhimurium (O52765), Mesocricetus auratus (P07178), Saccharomyces cerevisiae (P07263), Homo sapiens (P12081), Homo sapiens (P49590), Streptococcus dysgalactiae subsp. equisimilis (P30053), Caenorhabditis elegans (P34183), Haemophilus influenzae (P43823), Mycobacterium leprae (P46696), Mycoplasma genitalium (P47281), Porphyra purpurea (P51348), Thermus thermophilus (P56194), Thermus thermophilus, Helicobacter pylori (P56455), Escherichia coli (P60906), Escherichia coli, Takifugu rubripes (P70076), Mycoplasma pneumoniae (P75069), Oryza sativa (P93422), Mycobacterium tuberculosis (P9WFV5), Synechococcus sp. (Q55267), Synechocystis sp. (Q55653), Methanocaldococcus jannaschii (Q58406), Mus musculus (Q61035), Mycobacterium tuberculosis H37Rv (P9WFV5)
Manually annotated by BRENDA team
Felden, B.; Giege, R.
Resected RNA pseudoknots and their recognition by histidyl-tRNA synthetase
Proc. Natl. Acad. Sci. USA
95
10431-10436
1998
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Rosen, A.E.; Brooks, B.S.; Guth, E.; Francklyn, C.S.; Musier-Forsyth, K.
Evolutionary conservation of a functionally important backbone phosphate group critical for aminoacylation of histidine tRNAs
RNA
12
1315-1322
2006
Saccharomyces cerevisiae, Escherichia coli
Manually annotated by BRENDA team
Su, D.; Lieberman, A.; Lang, B.F.; Simonovic, M.; Soell, D.; Ling, J.
An unusual tRNAThr derived from tRNAHis reassigns in yeast mitochondria the CUN codons to threonine
Nucleic Acids Res.
39
4866-4874
2011
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Lee, Y.H.; Chang, C.P.; Cheng, Y.J.; Kuo, Y.Y.; Lin, Y.S.; Wang, C.C.
Evolutionary gain of highly divergent tRNA specificities by two isoforms of human histidyl-tRNA synthetase
Cell. Mol. Life Sci.
74
2663-2677
2017
Bacillus subtilis, Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team