ID   KHSE_BRUO2              Reviewed;         326 AA.
AC   A5VP46;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=BOV_0481;
OS   Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=444178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25840 / 63/290 / NCTC 10512;
RX   PubMed=19436743; DOI=10.1371/journal.pone.0005519;
RA   Tsolis R.M., Seshadri R., Santos R.L., Sangari F.J., Lobo J.M.,
RA   de Jong M.F., Ren Q., Myers G., Brinkac L.M., Nelson W.C., Deboy R.T.,
RA   Angiuoli S., Khouri H., Dimitrov G., Robinson J.R., Mulligan S.,
RA   Walker R.L., Elzer P.E., Hassan K.A., Paulsen I.T.;
RT   "Genome degradation in Brucella ovis corresponds with narrowing of its host
RT   range and tissue tropism.";
RL   PLoS ONE 4:E5519-E5519(2009).
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; CP000708; ABQ61511.1; -; Genomic_DNA.
DR   RefSeq; WP_005978415.1; NC_009505.1.
DR   AlphaFoldDB; A5VP46; -.
DR   SMR; A5VP46; -.
DR   EnsemblBacteria; ABQ61511; ABQ61511; BOV_0481.
DR   GeneID; 45123956; -.
DR   KEGG; bov:BOV_0481; -.
DR   HOGENOM; CLU_053300_1_0_5; -.
DR   OMA; DPTHFER; -.
DR   PhylomeDB; A5VP46; -.
DR   UniPathway; UPA00050; UER00064.
DR   Proteomes; UP000006383; Chromosome I.
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..326
FT                   /note="Homoserine kinase"
FT                   /id="PRO_1000022576"
SQ   SEQUENCE   326 AA;  36574 MW;  E3B0264713512E37 CRC64;
     MAVYTDINEI ELGAFLRHYD IGTLTSYKGI AEGVENSNYL LHTSSGSFIL TLYEKRTNRE
     DLPFFLGLMQ HLAKRGLECP QPVVRNDGAM IGQLAGRPAA IVTFLEGMWM RRPTVAHCEA
     VGEGLAHMHL AGADFPMRRR NGLTLPDWRP LWNLSRKCAD TVEQGLVAET EADLDFLEKN
     WPADLPQGVI HADLFPDNAF FLGDRLSGFI DFYFACTDIL AYDVAVCLNA WCFEKDFSYN
     RTKGAALLRG YTSVRPLSEA EADALPVLAR GAAVRFMLTR LYDWLTVPAG SFVVKKDPME
     YVRGMRFHRQ IESAAEYGLE MQEVAA