Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P00547 (KHSE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Homoserine kinase

Short name=HK
Short name=HSK
EC=2.7.1.39
Gene names
Name:thrB
Ordered Locus Names:b0003, JW0002
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length310 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.7

Catalytic activity

ATP + L-homoserine = ADP + O-phospho-L-homoserine. Ref.7

Pathway

Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 4/5. HAMAP-Rule MF_00384

Subcellular location

Cytoplasm Probable HAMAP-Rule MF_00384.

Sequence similarities

Belongs to the GHMP kinase family. Homoserine kinase subfamily.

Biophysicochemical properties

Kinetic parameters:

The catalytic efficiency is 500-fold higher with L-homoserine than with D-homoserine as substrate.

KM=0.14 mM for L-homoserine Ref.7

KM=31.8 mM for D-homoserine

KM=0.13 mM for ATP

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Threonine biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processthreonine biosynthetic process

Inferred from mutant phenotype PubMed 4148765PubMed 4364333. Source: EcoCyc

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

homoserine kinase activity

Inferred from direct assay PubMed 177283. Source: EcoCyc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 310310Homoserine kinase HAMAP-Rule MF_00384
PRO_0000156567

Regions

Nucleotide binding91 – 10111ATP Potential

Experimental info

Mutagenesis1391H → L: 35-fold decrease in kinase activity. Ref.7
Mutagenesis2031H → L: 2-fold decrease in kinase activity but nearly no change in substrates affinity. Ref.7
Mutagenesis2061H → Q: 3500-fold decrease in kinase activity. Ref.7
Mutagenesis2351R → H: 250-fold decrease in kinase activity but no change in substrates affinity. Ref.7
Mutagenesis2351R → L: 26200-fold decrease in catalytic efficiency. Ref.7

Sequences

Sequence LengthMass (Da)Tools
P00547 [UniParc].

Last modified April 1, 1993. Version 2.
Checksum: 0F225F9F1B634BE8

FASTA31033,624
        10         20         30         40         50         60 
MVKVYAPASS ANMSVGFDVL GAAVTPVDGA LLGDVVTVEA AETFSLNNLG RFADKLPSEP 

        70         80         90        100        110        120 
RENIVYQCWE RFCQELGKQI PVAMTLEKNM PIGSGLGSSA CSVVAALMAM NEHCGKPLND 

       130        140        150        160        170        180 
TRLLALMGEL EGRISGSIHY DNVAPCFLGG MQLMIEENDI ISQQVPGFDE WLWVLAYPGI 

       190        200        210        220        230        240 
KVSTAEARAI LPAQYRRQDC IAHGRHLAGF IHACYSRQPE LAAKLMKDVI AEPYRERLLP 

       250        260        270        280        290        300 
GFRQARQAVA EIGAVASGIS GSGPTLFALC DKPETAQRVA DWLGKNYLQN QEGFVHICRL 

       310 
DTAGARVLEN 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the thrB gene of E. coli, and its two adjacent regions; the thrAB and thrBC junctions."
Cossart P., Katinka M., Yaniv M.
Nucleic Acids Res. 9:339-347(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Update on the nucleotide sequence of the thrB gene of E. coli."
Deborde D.C., Strange J.C., Wright B.E.
Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION TO 166-190.
[3]"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12.
[4]"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, 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.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[6]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]"Substrate specificity and identification of functional groups of homoserine kinase from Escherichia coli."
Huo X., Viola R.E.
Biochemistry 35:16180-16185(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A HOMOSERINE KINASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS, MUTAGENESIS OF HIS-139; HIS-203; HIS-206 AND ARG-235.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L13601 Genomic DNA. Translation: AAA20618.1.
U14003 Genomic DNA. Translation: AAA97302.1.
U00096 Genomic DNA. Translation: AAC73114.1.
AP009048 Genomic DNA. Translation: BAB96580.2.
PIRKIECM. S56630.
RefSeqNP_414544.1. NC_000913.3.
YP_488309.1. NC_007779.1.

3D structure databases

ProteinModelPortalP00547.
SMRP00547. Positions 2-290.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP00547. 2 interactions.
STRING511145.b0003.

Chemistry

BindingDBP00547.

2D gel databases

SWISS-2DPAGEP00547.

Proteomic databases

PaxDbP00547.
PRIDEP00547.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73114; AAC73114; b0003.
BAB96580; BAB96580; BAB96580.
GeneID12932940.
947498.
KEGGecj:Y75_p0003.
eco:b0003.
PATRIC32115101. VBIEscCol129921_0002.

Organism-specific databases

EchoBASEEB0992.
EcoGeneEG10999. thrB.

Phylogenomic databases

eggNOGCOG0083.
HOGENOMHOG000247198.
KOK00872.
OMANVACGFD.
OrthoDBEOG6DG2WK.
PhylomeDBP00547.
ProtClustDBPRK01212.

Enzyme and pathway databases

BioCycEcoCyc:HOMOSERKIN-MONOMER.
ECOL316407:JW0002-MONOMER.
MetaCyc:HOMOSERKIN-MONOMER.
UniPathwayUPA00050; UER00064.

Gene expression databases

GenevestigatorP00547.

Family and domain databases

Gene3D3.30.230.10. 1 hit.
3.30.70.890. 1 hit.
HAMAPMF_00384. Homoser_kinase.
InterProIPR013750. GHMP_kinase_C_dom.
IPR006204. GHMP_kinase_N_dom.
IPR006203. GHMP_knse_ATP-bd_CS.
IPR000870. Homoserine_kinase.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view]
PfamPF08544. GHMP_kinases_C. 1 hit.
PF00288. GHMP_kinases_N. 1 hit.
[Graphical view]
PIRSFPIRSF000676. Homoser_kin. 1 hit.
SUPFAMSSF54211. SSF54211. 1 hit.
SSF55060. SSF55060. 1 hit.
TIGRFAMsTIGR00191. thrB. 1 hit.
PROSITEPS00627. GHMP_KINASES_ATP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP00547.

Entry information

Entry nameKHSE_ECOLI
AccessionPrimary (citable) accession number: P00547
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1993
Last modified: April 16, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene