ID   KHSE_BURCM              Reviewed;         332 AA.
AC   Q0BAN2;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=Bamb_3235;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS   (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-244 / AMMD;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA   Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-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; CP000441; ABI88791.1; -; Genomic_DNA.
DR   RefSeq; WP_011658283.1; NZ_CP009799.1.
DR   AlphaFoldDB; Q0BAN2; -.
DR   SMR; Q0BAN2; -.
DR   STRING; 339670.Bamb_3235; -.
DR   EnsemblBacteria; ABI88791; ABI88791; Bamb_3235.
DR   GeneID; 44693888; -.
DR   KEGG; bam:Bamb_3235; -.
DR   eggNOG; COG2334; Bacteria.
DR   OMA; DPTHFER; -.
DR   UniPathway; UPA00050; UER00064.
DR   Proteomes; UP000000662; 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_0000300786"
SQ   SEQUENCE   332 AA;  37226 MW;  EF19B5F4C99BA032 CRC64;
     MAVFTAVSDS DLAQWMRHYE LGDVLAFRGI PSGIENSNFF LTTTRGEYVL TIFEKLTAEQ
     LPFYLDLMRH LASHGVPVPD PIPRDDGALF GLLHGKPAAI VTKLDGAAEL APGIEHCIEV
     GQMLARLHLA GRDYARYQPN LRSLPWWREN VPAIVPFVSD AQRTLLEGEL AHQAAFFASD
     DYAALPSGPC HCDLFRDNVL FAHAAPGTGH DVRLGGFFDF YFAGCDKWLF DVAVTVNDWC
     VDLATGVLDV ARADALLRAY QTVRPFTAPE RRHWSDMLRA GAYRFWVSRL YDFYLPRAAE
     MLKPHDPGHF ERILRERIAN TPALPETHTA CN