Identification
Name:Homoserine kinase
Synonyms:
  • HK
  • HSK
Gene Name:thrB
Enzyme Class:
Biological Properties
General Function:Involved in ATP binding
Specific Function:Catalyzes the ATP-dependent phosphorylation of L- homoserine to L-homoserine phosphate. Is also able to phosphorylate the hydroxy group on gamma-carbon of L-homoserine analogs when the functional group at the alpha-position is a carboxyl, an ester, or even a hydroxymethyl group. Neither L- threonine nor L-serine are substrates of the enzyme
Cellular Location:Cytoplasm (Probable)
SMPDB Pathways:
  • Secondary Metabolites: threonine biosynthesis from aspartate PW000976
  • threonine biosynthesis PW000817
KEGG Pathways:
  • Glycine, serine and threonine metabolism ec00260
  • Metabolic pathways eco01100
  • Microbial metabolism in diverse environments ec01120
KEGG Reactions:
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
SMPDB Reactions:
1.0L-Homoserine+1.0Thumb+1.0Thumb1.0Adenosine diphosphate+1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Homoserine + 1.0Adenosine triphosphate + 1.0L-Homoserine → 1.0Adenosine diphosphate + 1.0Hydrogen ion + 1.0O-Phosphohomoserine + 1.0ADP
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
Complex Reactions:
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB02251L-HomoserineMetaboCard
ECMDB03484O-PhosphohomoserineMetaboCard
GO Classification:
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
binding
catalytic activity
homoserine kinase activity
kinase activity
nucleoside binding
phosphotransferase activity, alcohol group as acceptor
purine nucleoside binding
transferase activity
transferase activity, transferring phosphorus-containing groups
Process
aspartate family amino acid metabolic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular metabolic process
metabolic process
phosphate metabolic process
phosphorus metabolic process
phosphorylation
threonine metabolic process
Gene Properties
Blattner:b0003
Gene OrientationClockwise
Centisome Percentage:0.06
Left Sequence End2801
Right Sequence End3733
Gene Sequence:
>933 bp
ATGGTTAAAGTTTATGCCCCGGCTTCCAGTGCCAATATGAGCGTCGGGTTTGATGTGCTC
GGGGCGGCGGTGACACCTGTTGATGGTGCATTGCTCGGAGATGTAGTCACGGTTGAGGCG
GCAGAGACATTCAGTCTCAACAACCTCGGACGCTTTGCCGATAAGCTGCCGTCAGAACCA
CGGGAAAATATCGTTTATCAGTGCTGGGAGCGTTTTTGCCAGGAACTGGGTAAGCAAATT
CCAGTGGCGATGACCCTGGAAAAGAATATGCCGATCGGTTCGGGCTTAGGCTCCAGTGCC
TGTTCGGTGGTCGCGGCGCTGATGGCGATGAATGAACACTGCGGCAAGCCGCTTAATGAC
ACTCGTTTGCTGGCTTTGATGGGCGAGCTGGAAGGCCGTATCTCCGGCAGCATTCATTAC
GACAACGTGGCACCGTGTTTTCTCGGTGGTATGCAGTTGATGATCGAAGAAAACGACATC
ATCAGCCAGCAAGTGCCAGGGTTTGATGAGTGGCTGTGGGTGCTGGCGTATCCGGGGATT
AAAGTCTCGACGGCAGAAGCCAGGGCTATTTTACCGGCGCAGTATCGCCGCCAGGATTGC
ATTGCGCACGGGCGACATCTGGCAGGCTTCATTCACGCCTGCTATTCCCGTCAGCCTGAG
CTTGCCGCGAAGCTGATGAAAGATGTTATCGCTGAACCCTACCGTGAACGGTTACTGCCA
GGCTTCCGGCAGGCGCGGCAGGCGGTCGCGGAAATCGGCGCGGTAGCGAGCGGTATCTCC
GGCTCCGGCCCGACCTTGTTCGCTCTGTGTGACAAGCCGGAAACCGCCCAGCGCGTTGCC
GACTGGTTGGGTAAGAACTACCTGCAAAATCAGGAAGGTTTTGTTCATATTTGCCGGCTG
GATACGGCGGGCGCACGAGTACTGGAAAACTAA
Protein Properties
Pfam Domain Function:
Protein Residues:310
Protein Molecular Weight:33623
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Homoserine kinase
MVKVYAPASSANMSVGFDVLGAAVTPVDGALLGDVVTVEAAETFSLNNLGRFADKLPSEP
RENIVYQCWERFCQELGKQIPVAMTLEKNMPIGSGLGSSACSVVAALMAMNEHCGKPLND
TRLLALMGELEGRISGSIHYDNVAPCFLGGMQLMIEENDIISQQVPGFDEWLWVLAYPGI
KVSTAEARAILPAQYRRQDCIAHGRHLAGFIHACYSRQPELAAKLMKDVIAEPYRERLLP
GFRQARQAVAEIGAVASGISGSGPTLFALCDKPETAQRVADWLGKNYLQNQEGFVHICRL
DTAGARVLEN
References
External Links:
ResourceLink
Uniprot ID:P00547
Uniprot Name:KHSE_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674277
Ecogene ID:EG10999
Ecocyc:EG10999
ColiBase:b0003
Kegg Gene:b0003
EchoBASE ID:EB0992
CCDB:KHSE_ECOLI
BacMap:16127997
General Reference:
  • 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
  • Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L., Blattner, F. R. (1995). "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Nucleic Acids Res 23:2105-2119. Pubmed: 7610040
  • Cossart, P., Katinka, M., Yaniv, M. (1981). "Nucleotide sequence of the thrB gene of E. coli, and its two adjacent regions; the thrAB and thrBC junctions." Nucleic Acids Res 9:339-347. Pubmed: 6259626
  • 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
  • Huo, X., Viola, R. E. (1996). "Substrate specificity and identification of functional groups of homoserine kinase from Escherichia coli." Biochemistry 35:16180-16185. Pubmed: 8973190
  • Yura, T., Mori, H., Nagai, H., Nagata, T., Ishihama, A., Fujita, N., Isono, K., Mizobuchi, K., Nakata, A. (1992). "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Nucleic Acids Res 20:3305-3308. Pubmed: 1630901