Histidyl-tRNA synthetase (P60906)

Identification
Name:Histidyl-tRNA synthetase
Synonyms:
  • Histidine--tRNA ligase
  • HisRS
Gene Name:hisS
Enzyme Class:
Biological Properties
General Function:Involved in nucleotide binding
Specific Function:ATP + L-histidine + tRNA(His) = AMP + diphosphate + L-histidyl-tRNA(His)
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0tRNA(His)+1.0tRNA(His) ↔ 1.0Thumb+1.0L-Histidyl-tRNA(His)+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0L-Histidine + 1.0tRNA(His) + 1.0tRNA(His) ↔ 1.0Adenosine monophosphate + 1.0L-Histidyl-tRNA(His) + 1.0Pyrophosphate + 1.0L-Histidyl-tRNA(His)
ReactionCard
1.0Thumb+1.0Thumb+1.0tRNA(His) ↔ 1.0Thumb+1.0Thumb+1.0L-Histidyl-tRNA(His)
1.0Adenosine triphosphate + 1.0L-Histidine + 1.0tRNA(His) ↔ 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-Histidyl-tRNA(His)
ReactionCard
SMPDB Reactions:
1.0L-Histidine+1.0Thumb+1.0Thumb+1.0tRNA(His)+1.0Thumb → 1.0Thumb+1.0Pyrophosphate+1.0L-histidyl-tRNA(His)
1.0L-Histidine + 1.0Adenosine triphosphate + 1.0Hydrogen ion + 1.0tRNA(His) + 1.0L-Histidine → 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-histidyl-tRNA(His)
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0tRNA(His) → 1.0Thumb+1.0Thumb+1.0L-histidyl-tRNA(His)
1.0Adenosine triphosphate + 1.0L-Histidine + 1.0tRNA(His) → 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-histidyl-tRNA(His)
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00177L-HistidineMetaboCard
ECMDB23780L-Histidyl-tRNA(His)MetaboCard
ECMDB04142PyrophosphateMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
aminoacyl-tRNA ligase activity
ATP binding
binding
catalytic activity
histidine-tRNA ligase activity
ligase activity
ligase activity, forming aminoacyl-tRNA and related compounds
ligase activity, forming carbon-oxygen bonds
nucleoside binding
nucleotide binding
purine nucleoside binding
Process
biosynthetic process
cellular macromolecule biosynthetic process
cellular macromolecule metabolic process
histidyl-tRNA aminoacylation
macromolecule biosynthetic process
macromolecule metabolic process
metabolic process
ncRNA metabolic process
RNA metabolic process
translation
tRNA aminoacylation
tRNA aminoacylation for protein translation
tRNA metabolic process
Gene Properties
Blattner:b2514
Gene OrientationCounterclockwise
Centisome Percentage:56.84
Left Sequence End2637323
Right Sequence End2638597
Gene Sequence:
>1275 bp
ATGACAGATAAACGCAAAGATGGCTCAGGCAAATTGCTGTATTGCTCTTTTTGCGGCAAA
AGCCAGCATGAAGTGCGCAAGCTGATTGCCGGTCCATCCGTGTATATCTGCGACGAATGT
GTTGATTTATGTAACGACATCATTCGCGAAGAGATTAAAGAAGTTGCACCGCATCGTGAA
CGCAGTGCGCTACCGACGCCGCATGAAATTCGCAACCACCTGGACGATTACGTTATCGGC
CAGGAACAGGCGAAAAAAGTGCTGGCGGTCGCGGTATACAACCATTACAAACGTCTGCGC
AACGGCGATACCAGCAATGGCGTCGAGTTGGGCAAAAGTAACATTCTGCTGATCGGTCCG
ACCGGTTCCGGTAAAACGCTGCTGGCTGAAACGCTGGCGCGCCTGCTGGATGTTCCGTTC
ACCATGGCCGACGCGACTACACTGACCGAAGCCGGTTATGTGGGTGAAGACGTTGAAAAC
ATCATTCAGAAGCTGTTGCAGAAATGCGACTACGATGTCCAGAAAGCACAGCGTGGTATT
GTCTACATCGATGAAATCGACAAGATTTCTCGTAAGTCAGACAACCCGTCCATTACCCGA
GACGTTTCCGGTGAAGGCGTACAGCAGGCACTGTTGAAACTGATCGAAGGTACGGTAGCT
GCTGTTCCACCGCAAGGTGGGCGTAAACATCCGCAGCAGGAATTCTTGCAGGTTGATACC
TCTAAGATCCTGTTTATTTGTGGCGGTGCGTTTGCCGGTCTGGATAAAGTGATTTCCCAC
CGTGTAGAAACCGGCTCCGGCATTGGTTTTGGCGCGACGGTAAAAGCGAAGTCCGACAAA
GCAAGCGAAGGCGAGCTGCTGGCGCAGGTTGAACCGGAAGATCTGATCAAGTTTGGTCTT
ATCCCTGAGTTTATTGGTCGTCTGCCGGTTGTCGCAACGTTGAATGAACTGAGCGAAGAA
GCTCTGATTCAGATCCTCAAAGAGCCGAAAAACGCCCTGACCAAGCAGTATCAGGCGCTG
TTTAATCTGGAAGGCGTGGATCTGGAATTCCGTGACGAGGCGCTGGATGCTATCGCTAAG
AAAGCGATGGCGCGTAAAACCGGTGCCCGTGGCCTGCGTTCCATCGTAGAAGCCGCACTG
CTCGATACCATGTACGATCTGCCGTCCATGGAAGACGTCGAAAAAGTGGTTATCGACGAG
TCGGTAATTGATGGTCAAAGCAAACCGTTGCTGATTTATGGCAAGCCGGAAGCGCAACAG
GCATCTGGTGAATAA
Protein Properties
Pfam Domain Function:
Protein Residues:424
Protein Molecular Weight:47029
Protein Theoretical pI:6
PDB File:1KMN
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Histidyl-tRNA synthetase
MAKNIQAIRGMNDYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRAIGEVT
DVVEKEMYTFEDRNGDSLTLRPEGTAGCVRAGIEHGLLYNQEQRLWYIGPMFRHERPQKG
RYRQFHQLGCEVFGLQGPDIDAELIMLTARWWRALGISEHVTLELNSIGSLEARANYRDA
LVAFLEQHKEKLDEDCKRRMYTNPLRVLDSKNPEVQALLNDAPALGDYLDEESREHFAGL
CKLLESAGIAYTVNQRLVRGLDYYNRTVFEWVTNSLGSQGTVCAGGRYDGLVEQLGGRAT
PAVGFAMGLERLVLLVQAVNPEFKADPVVDIYLVASGADTQSAAMALAERLRDELPGVKL
MTNHGGGNFKKQFARADKWGARVAVVLGESEVANGTAVVKDLRSGEQTAVAQDSVAAHLR
TLLG
References
External Links:
ResourceLink
Uniprot ID:P60906
Uniprot Name:SYH_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674578
PDB ID:1KMN
Ecogene ID:EG10453
Ecocyc:EG10453
ColiBase:b2514
Kegg Gene:b2514
EchoBASE ID:EB0448
CCDB:SYH_ECOLI
BacMap:16130439
General Reference:
  • Arnez, J. G., Augustine, J. G., Moras, D., Francklyn, C. S. (1997). "The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase." Proc Natl Acad Sci U S A 94:7144-7149. Pubmed: 9207058
  • Arnez, J. G., Harris, D. C., Mitschler, A., Rees, B., Francklyn, C. S., Moras, D. (1995). "Crystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate." EMBO J 14:4143-4155. Pubmed: 7556055
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Eisenbeis, S. J., Parker, J. (1982). "The nucleotide sequence of the promoter region of hisS, the structural gene for histidyl-tRNA synthetase." Gene 18:107-114. Pubmed: 6290315
  • Freedman, R., Gibson, B., Donovan, D., Biemann, K., Eisenbeis, S., Parker, J., Schimmel, P. (1985). "Primary structure of histidine-tRNA synthetase and characterization of hisS transcripts." J Biol Chem 260:10063-10068. Pubmed: 2991272
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Yamamoto, Y., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kimura, S., Kitagawa, M., Makino, K., Miki, T., Mitsuhashi, N., Mizobuchi, K., Mori, H., Nakade, S., Nakamura, Y., Nashimoto, H., Oshima, T., Oyama, S., Saito, N., Sampei, G., Satoh, Y., Sivasundaram, S., Tagami, H., Horiuchi, T., et, a. l. .. (1997). "Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." DNA Res 4:91-113. Pubmed: 9205837