ID   KHSE_RHOPT              Reviewed;         327 AA.
AC   B3Q6U2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=Rpal_4750;
OS   Rhodopseudomonas palustris (strain TIE-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=395960;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TIE-1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Emerson D.,
RA   Newman D.K., Roden E., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris TIE-1.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001096; ACF03241.1; -; Genomic_DNA.
DR   RefSeq; WP_012497493.1; NC_011004.1.
DR   AlphaFoldDB; B3Q6U2; -.
DR   SMR; B3Q6U2; -.
DR   EnsemblBacteria; ACF03241; ACF03241; Rpal_4750.
DR   KEGG; rpt:Rpal_4750; -.
DR   HOGENOM; CLU_053300_1_0_5; -.
DR   OMA; DPTHFER; -.
DR   OrthoDB; 1003984at2; -.
DR   BioCyc; RPAL395960:RPAL_RS23515-MON; -.
DR   UniPathway; UPA00050; UER00064.
DR   Proteomes; UP000001725; 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   Threonine biosynthesis; Transferase.
FT   CHAIN           1..327
FT                   /note="Homoserine kinase"
FT                   /id="PRO_1000115441"
SQ   SEQUENCE   327 AA;  35807 MW;  6574D68EDE5BAD80 CRC64;
     MAVYTDVAAD ELADFLSRYD IGDLLSYKGI AEGVENSNFL LHTSRGYFIL TLYEKRVARD
     DLPFFLSLMT HLADSGINCP QPVADREGRT LATLAGRPAA IISFLDGVWP RKPSVVHCAG
     VGQALAKMHL AGRDFAMKRA NALSVAGWRP LFAAAEARAD EVQPGLRDFL AAELSYLESG
     VWPSDLPQGL IHADLFPDNV FFIGDDVSGI IDFTFACNDL LAYDVAICLN AWCFEADHAF
     NVTKARALLS AYTRERPLDA AEQAALPLLA RGAALRFLLT RLVDWLNVPE GALVKPKDPM
     EYVRKLRFQQ NVAGIRDYGV EIAGAVA