ID   KHSE_THEVB              Reviewed;         301 AA.
AC   Q8DI27;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=tlr1765;
OS   Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC   Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX   PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA   Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA   Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   DNA Res. 9:123-130(2002).
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; BA000039; BAC09317.1; -; Genomic_DNA.
DR   RefSeq; NP_682555.1; NC_004113.1.
DR   RefSeq; WP_011057602.1; NC_004113.1.
DR   AlphaFoldDB; Q8DI27; -.
DR   SMR; Q8DI27; -.
DR   STRING; 197221.22295491; -.
DR   EnsemblBacteria; BAC09317; BAC09317; BAC09317.
DR   KEGG; tel:tlr1765; -.
DR   PATRIC; fig|197221.4.peg.1846; -.
DR   eggNOG; COG0083; Bacteria.
DR   OMA; CANRIPH; -.
DR   OrthoDB; 610857at2; -.
DR   UniPathway; UPA00050; UER00064.
DR   Proteomes; UP000000440; 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; Reference proteome; Threonine biosynthesis;
KW   Transferase.
FT   CHAIN           1..301
FT                   /note="Homoserine kinase"
FT                   /id="PRO_0000156622"
FT   BINDING         86..96
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00384"
SQ   SEQUENCE   301 AA;  32174 MW;  25543A4CA3381E23 CRC64;
     MITVVTVPAT TANLGPGFDC LGAALTLTNR FTFSLSDRPH VSVRGPEAAA VSSGPNNLAY
     RAYSRFYEYL GREAPPVYLE IDLRVPLARG LGSSATAIIG GLVGANRLAG FPLSHTEVLE
     LAIEMEGHPD NVVPALLGGC RLAVQEDAGG WHWLEIPWDQ DVVPILAIPD FELATETARE
     VLPPHCAYGD AIFNISHLGA LLRGLETGQR EWLQLALADR LHQPYRQSLI KGYPDLHRAA
     LEAGAHGLVI SGAGPTLLAL GDPVTASAIA TALKETWAKF DVQAQVEILA IQHQGTTVCD
     R