ID   KHSE_CUPMC              Reviewed;         328 AA.
AC   Q1LK22;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=Rmet_2627;
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(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; CP000352; ABF09504.1; -; Genomic_DNA.
DR   RefSeq; WP_011517203.1; NC_007973.1.
DR   AlphaFoldDB; Q1LK22; -.
DR   SMR; Q1LK22; -.
DR   STRING; 266264.Rmet_2627; -.
DR   EnsemblBacteria; ABF09504; ABF09504; Rmet_2627.
DR   KEGG; rme:Rmet_2627; -.
DR   eggNOG; COG2334; Bacteria.
DR   HOGENOM; CLU_053300_0_0_4; -.
DR   OMA; DPTHFER; -.
DR   OrthoDB; 1003984at2; -.
DR   UniPathway; UPA00050; UER00064.
DR   Proteomes; UP000002429; Chromosome.
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   Reference proteome; Threonine biosynthesis; Transferase.
FT   CHAIN           1..328
FT                   /note="Homoserine kinase"
FT                   /id="PRO_0000300800"
SQ   SEQUENCE   328 AA;  37361 MW;  141C2E87C7C259EB CRC64;
     MAVFTTVSQD EIARWLLDYD LGEVRALRGI ASGIENSNFF LTMEQDGVTR EYVLTIFERL
     QFDQLPYYLH LMDHLARHGI CVPAPMPARD GEILRELKGK PATIVTRLPG ASQLAPQPDH
     CAEVGAMLAR MHIAGQDYPR KQPNLRSLAW WQQTTPEITP FLDAAQRKLL TEEIAHQTAF
     FGSGDYAALQ GGPCHCDLFR DNALFDTDSA GNHRLGGFFD FYFAGDDKWL FDLAVTVNDW
     CIDLATGTID MERAQAMLRA YHAVRPLTAV EAAHWQDMLR AGALRFWVSR LWDFYLPREA
     DMLQPHDPTH FERILRRRID DAAALPWI