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P04948 (KHSE_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:BSU32240
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length309 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
Reference 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 – 309309Homoserine kinase HAMAP MF_00384
PRO_0000156554

Regions

Nucleotide binding91 – 10111ATP Potential

Experimental info

Sequence conflict57 – 582PA → R in CAA28271. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P04948 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 0661A7DEFAA5FFAC

FASTA30933,324
        10         20         30         40         50         60 
MNEADMLFSV TVPGSTANLG PGFDSVGMAL SRYLKLTVFE SDKWSFEAET ETVAGIPAGT 

        70         80         90        100        110        120 
DNLIYQVAKR TADLYGKEMP PVHVKVWSDI PLARGLGSSA AAIVAAIELA DELCGLKLSE 

       130        140        150        160        170        180 
ADKLHLASLE EGHPDNAGAS LVGGLVIGLH EDDETQMIRV PNADIDVVVV IPFYEVLTRD 

       190        200        210        220        230        240 
ARDVLPKEFP YADAVKASAV SNILIAAIMS KDWPLVGKIM KKDMFHQPYR AMLVPELSKV 

       250        260        270        280        290        300 
EHVAEMKGAY GTALSGAGPT ILVMTEKGKG EELKEQLALH FPHCEVDALT VPKEGSIIER 


NPLYQVKSV

« Hide

References

« Hide 'large scale' references
[1]"Evolution of biosynthetic pathways: a common ancestor for threonine synthase, threonine dehydratase and D-serine dehydratase."
Parsot C.
EMBO J. 5:3013-3019(1986) [PubMed: 3098560] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X04603 Genomic DNA. Translation: CAA28271.1.
AL009126 Genomic DNA. Translation: CAB15214.1.
PIRH69722.
RefSeqNP_391104.1. NC_000964.3.

3D structure databases

ProteinModelPortalP04948.
SMRP04948. Positions 7-302.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000000953; EBBACP00000000953; EBBACG00000000951.
GeneID936665.
GenomeReviewsGene locus BSU32240 in contig AL009126_GR.
KEGGbsu:BSU32240.
NMPDRfig|224308.1.peg.3230.
PATRIC18978420. VBIBacSub10457_3373.

Organism-specific databases

GenoListBSU32240. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000000874.
HOGENOMHBG646290.
OMADRLHQPY.
PhylomeDBP04948.
ProtClustDBPRK01212.

Enzyme and pathway databases

BioCycBSUB:BSU32240-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_BACSU
AccessionPrimary (citable) accession number: P04948
Secondary accession number(s): O32121
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: May 30, 2000
Last modified: January 25, 2012
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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