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Information on EC 6.1.1.21 - histidine-tRNA ligase and Organism(s) Thermus thermophilus and UniProt Accession P56194

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Thermus thermophilus
UNIPROT: P56194 not found.
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The taxonomic range for the selected organisms is: Thermus thermophilus
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, histidine-trna ligase, class ii histidyl-trna synthetase, hars1, mitochondrial histidyl trna synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Histidine translase
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histidine-tRNA ligase
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histidine-tRNA ligase homolog
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Histidyl-transfer ribonucleate synthetase
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Histidyl-tRNA synthetase
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Synthetase, histidyl-transfer ribonucleate
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HisRS
Histidine translase
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-
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Histidine--tRNA ligase
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-
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Histidine--tRNA ligase homolog
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-
-
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histidyl tRNA synthetase
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Histidyl-transfer ribonucleate synthetase
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-
-
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Histidyl-tRNA synthetase
Jo-1
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-
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Jo-1 antigen
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-
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Synthetase, histidyl-transfer ribonucleate
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-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-histidine + tRNAHis = AMP + diphosphate + L-histidyl-tRNAHis
show the reaction diagram
2-step mechanism, elucidation of structure-activity relationship, the N-terminal catalytic domain contains the six-stranded antiparallel beta-sheet and the three motifs characteristics of class II aaRS, a HisRS-specific helical domain inserted between motifs 2 and 3 that may contact the acceptor stem of the tRNA, a C-terminal alpha/beta domain may be involved in the recognition of the anticodon stem and loop of tRNAHis
ATP + L-histidine + tRNAHis = AMP + diphosphate + L-histidyl-tRNAHis
show the reaction diagram
relation between the conservation of active site residues and the molecular mechanism of aminoacylation reaction, relevant reaction coordinate and the orientation of the catalytic residue, Arg259, model of active site with the substrates, Mg2+ ions and water, overview. Calculation of the transition state structures of the activation step of aminoacylation reaction using the combined ab-initio/semi-empirical calculation
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
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-
-
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Aminoacylation
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-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
L-histidine:tRNAHis ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9068-78-4
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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-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
show the reaction diagram
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
show the reaction diagram
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
the enzyme is involved in several regulatory mechanisms of the cell metabolism
-
ir
ATP + L-histidine + tRNAHis
AMP + diphosphate + L-histidyl-tRNAHis
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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the conserved active site residues near the reaction center, Thr60, Val62, Pro82, Glu83, Gly84, Arg113, Gln127, Arg259, Gly260, Leu261, Ala284 and Ala306, which have a major role in the reaction mechanism and catalysis, retain their specific position and orientation relative to the substrate in the three species, Escherichia coli, Thermus thermophilus, and Staphylococcus aureus, modelling, reaction emchanism, detailed overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
47100
x * 47100, amino acid sequence determination
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 47100, amino acid sequence determination
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis
enzyme complexed with tRNAHis, L-histidine, and AMPPNP, hanging drop vapor diffusion method, using 5% (w/v) PEG 4000 and 0.1 M NaOAc (pH4.5)
enzyme in complex with histidine
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HisRS and its complex with histidine and its cognate tRNAHis
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
325-328Del
the mutant shows about 20% of wild type activity
328insTTET
the mutant shows about 80% of wild type activity
E388A
the mutant shows about 15% of wild type activity
G286A
the mutant shows about 2% of wild type activity
G72V
the mutant shows about 50% of wild type activity
G72V/G73V
the mutant shows about 15% of wild type activity
K209A
the mutant shows about 80% of wild type activity
K397Q
the mutant shows about 10% of wild type activity
Q404A
the mutant shows about 90% of wild type activity
R115A
the mutant shows about 20% of wild type activity
R120A
the mutant shows about 8% of wild type activity
R122A
the mutant shows about 15% of wild type activity
R122K
the mutant shows about 55% of wild type activity
R197A
the mutant shows about 50% of wild type activity
R7A
the mutant shows about 20% of wild type activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yaremchuk, A.D.; Cusack, S.; Aberg, A.; Gudzera, O.; Kryklivyi, I.; Tukalo, M.
Crystallization of Thermus thermophilus histidyl-tRNA synthetase and its complex with tRNAHis
Proteins Struct. Funct. Genet.
22
426-428
1995
Thermus thermophilus
Manually annotated by BRENDA team
Aberg, A.; Yaremchuk, A.; Tukalo, M.; Rasmussen, B.; Cusack, S.
Crystal structure analysis of the activation of histidine by Thermus thermophilus histidyl-tRNA synthetase
Biochemistry
36
3084-3094
1997
Thermus thermophilus
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
Banik, S.D.; Nandi, N.
Influence of the conserved active site residues of histidyl tRNA synthetase on the mechanism of aminoacylation reaction
Biophys. Chem.
158
61-72
2011
Escherichia coli, Thermus thermophilus, Staphylococcus aureus
Manually annotated by BRENDA team
Dutta, S.; Kundu, S.; Saha, A.; Nandi, N.
Dynamics of the active site loops in catalyzing aminoacylation reaction in seryl and histidyl tRNA synthetases
J. Biomol. Struct. Dyn.
36
878-892
2018
Thermus thermophilus
Manually annotated by BRENDA team
Tian, Q.; Wang, C.; Liu, Y.; Xie, W.
Structural basis for recognition of G-1-containing tRNA by histidyl-tRNA synthetase
Nucleic Acids Res.
43
2980-2990
2015
Thermus thermophilus (P62374)
Manually annotated by BRENDA team