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Q1B535 (KHSE_MYCSS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:Mmcs_3894
OrganismMycobacterium sp. (strain MCS) [Complete proteome] [HAMAP]
Taxonomic identifier164756 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length314 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate By similarity. HAMAP MF_00384

Catalytic activity

ATP + L-homoserine = ADP + O-phospho-L-homoserine. HAMAP MF_00384

Pathway

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

Subcellular location

Cytoplasm Potential HAMAP MF_00384.

Sequence similarities

Belongs to the GHMP kinase family. Homoserine kinase subfamily.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

homoserine kinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 314314Homoserine kinase HAMAP MF_00384
PRO_1000049150

Regions

Nucleotide binding95 – 10511ATP Potential

Sequences

Sequence LengthMass (Da)Tools
Q1B535 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: A80F06311BA8B9A6

FASTA31431,814
        10         20         30         40         50         60 
MTQTLPAGLT ATATVAASSA NLGPGFDSLG LALSLYDEIV VETVDSGLTV TVEGEGAGQV 

        70         80         90        100        110        120 
ALDSSHLVVR AIEAGLRATG CIAPGLVVRC RNDIPHSRGL GSSAAAVVGG LAAANGLVSQ 

       130        140        150        160        170        180 
TDWTPLTVEQ LIQLSSAFEG HPDNAAAAVL GGAVVTWTDG AGAQARYAAA PLRVHPDIHL 

       190        200        210        220        230        240 
FPAIPQQRSS TAETRVLLPD TVSHTDARFN LSRAALLVVA LTERPDLLMA ATEDVLHQPQ 

       250        260        270        280        290        300 
RAAAMPASAE FLRVLRGCGV AAVLSGAGPA VIALSTEPVL PAEAVEFGIA NGFTIAEMAV 

       310 
GDGVRWSTGV AAGR

« Hide

References

[1]"Complete sequence of chromosome of Mycobacterium sp. MCS."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E. expand/collapse author list , Miller C.D., Hughes J.E., Anderson A.J., Sims R.C., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MCS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000384 Genomic DNA. Translation: ABG09999.1.
RefSeqYP_641055.1. NC_008146.1.

3D structure databases

ProteinModelPortalQ1B535.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1B535.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000061070; EBMYCP00000059237; EBMYCG00000061065.
GeneID4112724.
GenomeReviewsGene locus Mmcs_3894 in contig CP000384_GR.
KEGGmmc:Mmcs_3894.
PATRIC18118121. VBIMycSp106721_3991.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0083.
GeneTreeEBGT00050000016145.
HOGENOMHBG646290.
OMADRLHQPY.
ProtClustDBPRK01212.

Enzyme and pathway databases

BioCycMSP164756:MMCS_3894-MONOMER.

Family and domain databases

HAMAPMF_00384. Homoser_kinase.
[Tree]
InterProIPR006204. GHMP_kinase.
IPR013750. GHMP_kinase_C.
IPR006203. GHMP_knse_ATP-bd_CS.
IPR000870. Homoserine_kinase.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view]
Gene3DG3DSA:3.30.230.10. Ribosomal_S5_D2-type_fold. 1 hit.
KOK00872.
PfamPF08544. GHMP_kinases_C. 1 hit.
PF00288. GHMP_kinases_N. 1 hit.
[Graphical view]
PIRSFPIRSF000676. Homoser_kin. 1 hit.
PRINTSPR00958. HOMSERKINASE.
SUPFAMSSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.
TIGRFAMsTIGR00191. ThrB. 1 hit.
PROSITEPS00627. GHMP_KINASES_ATP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKHSE_MYCSS
AccessionPrimary (citable) accession number: Q1B535
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 11, 2006
Last modified: January 25, 2012
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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