ID   KHSE_CUPPJ              Reviewed;         330 AA.
AC   Q474D4;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Homoserine kinase {ECO:0000255|HAMAP-Rule:MF_00301};
DE            Short=HK {ECO:0000255|HAMAP-Rule:MF_00301};
DE            Short=HSK {ECO:0000255|HAMAP-Rule:MF_00301};
DE            EC=2.7.1.39 {ECO:0000255|HAMAP-Rule:MF_00301};
GN   Name=thrB {ECO:0000255|HAMAP-Rule:MF_00301}; OrderedLocusNames=Reut_A0870;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(2010).
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_00301};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00301}.
CC   -!- SIMILARITY: Belongs to the pseudomonas-type ThrB family.
CC       {ECO:0000255|HAMAP-Rule:MF_00301}.
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DR   EMBL; CP000090; AAZ60249.1; -; Genomic_DNA.
DR   RefSeq; WP_011297054.1; NC_007347.1.
DR   AlphaFoldDB; Q474D4; -.
DR   SMR; Q474D4; -.
DR   STRING; 264198.Reut_A0870; -.
DR   EnsemblBacteria; AAZ60249; AAZ60249; Reut_A0870.
DR   KEGG; reu:Reut_A0870; -.
DR   eggNOG; COG2334; Bacteria.
DR   HOGENOM; CLU_053300_0_0_4; -.
DR   OMA; DPTHFER; -.
DR   OrthoDB; 1003984at2; -.
DR   UniPathway; UPA00050; UER00064.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   CDD; cd05153; HomoserineK_II; 1.
DR   HAMAP; MF_00301; Homoser_kinase_2; 1.
DR   InterPro; IPR002575; Aminoglycoside_PTrfase.
DR   InterPro; IPR005280; Homoserine_kinase_II.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   Pfam; PF01636; APH; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   TIGRFAMs; TIGR00938; thrB_alt; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; ATP-binding; Kinase; Nucleotide-binding;
KW   Threonine biosynthesis; Transferase.
FT   CHAIN           1..330
FT                   /note="Homoserine kinase"
FT                   /id="PRO_0000300799"
SQ   SEQUENCE   330 AA;  37356 MW;  CA3F2EDA19F564F6 CRC64;
     MAVFTTVSHD EIASWLLDYD LGEVRELRGI ASGIENSNFF LTTEQDGRTR EYVLTIFERL
     TFDQLPYYLH LMAHLATRGI TVPAPIPARD GEILRALKGK PATIVTRLPG ASQLAPDAEH
     CAEVGDMLAR MHLAGQDYPR QQPNLRSLPW WQQTEAEIVP FLDAQQRTLL QQEIAHQAAF
     FGSADYAALP GGPCHCDLFR DNALFEEVGG HHRLGGFFDF YFAGNDKWLF DLAVTVNDWC
     IDLASGELDN ARAHAMVQAY HAVRPLSATE AAHWRDMLRA GALRFWVSRL WDFYLPREAD
     MLQPHDPTHF ERILRRRLAM TADAAALAWI