ID   KHSE_CHESB              Reviewed;         322 AA.
AC   Q11KC6;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 95.
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=Meso_0749;
OS   Chelativorans sp. (strain BNC1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Chelativorans.
OX   NCBI_TaxID=266779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BNC1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of chromosome of Mesorhizobium sp. BNC1.";
RL   Submitted (JUN-2006) 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; CP000390; ABG62149.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q11KC6; -.
DR   SMR; Q11KC6; -.
DR   STRING; 266779.Meso_0749; -.
DR   KEGG; mes:Meso_0749; -.
DR   eggNOG; COG2334; Bacteria.
DR   HOGENOM; CLU_053300_0_0_5; -.
DR   OrthoDB; 9777460at2; -.
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   Gene3D; 3.90.1200.10; -; 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   NCBIfam; TIGR00938; thrB_alt; 1.
DR   PANTHER; PTHR21064:SF6; APH DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR21064; UNCHARACTERIZED; 1.
DR   Pfam; PF01636; APH; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; ATP-binding; Kinase; Nucleotide-binding;
KW   Threonine biosynthesis; Transferase.
FT   CHAIN           1..322
FT                   /note="Homoserine kinase"
FT                   /id="PRO_0000300794"
SQ   SEQUENCE   322 AA;  36289 MW;  BB2B9EE2742386BB CRC64;
     MAVYTDISEE ELTAFLRHYP VGKLLSYKGI AEGTENSNYL LHTTAGAYIL TLYERRVDRS
     DLPFFLGLME HLARKGVSCP LPVKRLDDGL IGELAGRPAA LITFLEGMWM RRPTALHCGQ
     VGKALADLHQ AAEDFPLKRP NALGPEGWRR LWEGAKARAD EVEPGLAREV DAEFALLERD
     WPKDLPSGVI HADLFPDNVF FLGGELSGLI DFYFACNDLL AYDLATCLNA WCFEKDISYN
     LTKGAALLAG YQAVRPLTRE EIEMLPLLAR GSALRFMLTR LYDWLTIPDG ALVKKRDPLE
     YLRRLRFHRQ VRTASEYGIE LA
//