ID   KHSE_YERPS              Reviewed;         309 AA.
AC   Q66ET8;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Homoserine kinase {ECO:0000255|HAMAP-Rule:MF_00384};
DE            Short=HK {ECO:0000255|HAMAP-Rule:MF_00384};
DE            Short=HSK {ECO:0000255|HAMAP-Rule:MF_00384};
DE            EC=2.7.1.39 {ECO:0000255|HAMAP-Rule:MF_00384};
GN   Name=thrB {ECO:0000255|HAMAP-Rule:MF_00384}; OrderedLocusNames=YPTB0603;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
CC   -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of L-homoserine
CC       to L-homoserine phosphate. {ECO:0000255|HAMAP-Rule:MF_00384}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine;
CC         Xref=Rhea:RHEA:13985, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57476, ChEBI:CHEBI:57590, ChEBI:CHEBI:456216;
CC         EC=2.7.1.39; Evidence={ECO:0000255|HAMAP-Rule:MF_00384};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00384}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00384}.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. Homoserine kinase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00384}.
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DR   EMBL; BX936398; CAH19843.1; -; Genomic_DNA.
DR   RefSeq; WP_002209238.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q66ET8; -.
DR   SMR; Q66ET8; -.
DR   EnsemblBacteria; CAH19843; CAH19843; YPTB0603.
DR   GeneID; 66842976; -.
DR   KEGG; ypo:BZ17_1954; -.
DR   KEGG; yps:YPTB0603; -.
DR   PATRIC; fig|273123.14.peg.2079; -.
DR   OMA; CANRIPH; -.
DR   UniPathway; UPA00050; UER00064.
DR   Proteomes; UP000001011; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004413; F:homoserine kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.890; -; 1.
DR   HAMAP; MF_00384; Homoser_kinase; 1.
DR   InterPro; IPR013750; GHMP_kinase_C_dom.
DR   InterPro; IPR036554; GHMP_kinase_C_sf.
DR   InterPro; IPR006204; GHMP_kinase_N_dom.
DR   InterPro; IPR006203; GHMP_knse_ATP-bd_CS.
DR   InterPro; IPR000870; Homoserine_kinase.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   Pfam; PF08544; GHMP_kinases_C; 1.
DR   Pfam; PF00288; GHMP_kinases_N; 1.
DR   PIRSF; PIRSF000676; Homoser_kin; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55060; SSF55060; 1.
DR   TIGRFAMs; TIGR00191; thrB; 1.
DR   PROSITE; PS00627; GHMP_KINASES_ATP; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; ATP-binding; Cytoplasm; Kinase;
KW   Nucleotide-binding; Threonine biosynthesis; Transferase.
FT   CHAIN           1..309
FT                   /note="Homoserine kinase"
FT                   /id="PRO_0000156637"
FT   BINDING         91..101
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00384"
SQ   SEQUENCE   309 AA;  33231 MW;  175F39BEB5A7B416 CRC64;
     MVKIYAPASI GNVSVGFDVL GAAVSPIDGT LLGDCVSVTA AERFSLHNEG RFVSKLPDDP
     KQNIVYQCWE RFCQEMGKEI PVAMVLEKNM PIGSGLGSSA CSVVAGLMAM NEFCGQPLDK
     VTLLGMMGEL EGRVSGSIHF DNVAPCYLGG MQLILEQEGY ISQDVPGFSD WLWVMAYPGI
     KVSTAEARAI LPAQYRRQDC ITHGRNLAGF IHACHTQQPD LAAKMMKDVI AEPYRTQLLP
     GFAAARQAAQ DIGALACGIS GSGPTLFAVC NDQATAQRMA GWLQNHYLQN DEGFVHICRL
     DTAGARLLG