ID   KHSE_BURL3              Reviewed;         332 AA.
AC   Q393M6;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
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};
GN   OrderedLocusNames=Bcep18194_B2229;
OS   Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 /
OS   R18194 / 383).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=482957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia sp. 383.";
RL   Submitted (OCT-2005) 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; CP000152; ABB12340.1; -; Genomic_DNA.
DR   RefSeq; WP_011355822.1; NC_007511.1.
DR   AlphaFoldDB; Q393M6; -.
DR   SMR; Q393M6; -.
DR   EnsemblBacteria; ABB12340; ABB12340; Bcep18194_B2229.
DR   GeneID; 45098554; -.
DR   KEGG; bur:Bcep18194_B2229; -.
DR   PATRIC; fig|482957.22.peg.5989; -.
DR   HOGENOM; CLU_053300_0_0_4; -.
DR   OMA; DPTHFER; -.
DR   OrthoDB; 1003984at2; -.
DR   UniPathway; UPA00050; UER00064.
DR   Proteomes; UP000002705; Chromosome 2.
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..332
FT                   /note="Homoserine kinase"
FT                   /id="PRO_0000300789"
SQ   SEQUENCE   332 AA;  37266 MW;  23B3E844F8D52864 CRC64;
     MAVFTAVSDS DLAQWMRHYE LGDVLAFRGI PSGIENSNFF LTTTRGEYVL TIFEKLTAEQ
     LPFYLDLMSH LAGHGVPVPD PIPRDDGALF GMLHGKPAAI VTKLDGSAEL APGVEHCIEV
     GQMLARLHLA GRDYPRNQPN LRSLPWWQEN VPAIVPFITD EQRALLEGEL VHQAGFFASD
     DYAALPAGPC HCDLFRDNVL FAHAAPDTGH DVRLGGFFDF YFAGCDKWLF DVAVTVNDWC
     VDLATGVLDV ARADALLRAY QTVRPFTAEE RRHWSDMLRA GAYRFWVSRL YDFYLPRAAE
     MLKPHDPGHF ERILRERIAH TPALPEIQTA CN