ID   KHSE_BURCJ              Reviewed;         332 AA.
AC   B4EN17;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=BceJ2315_43540; ORFNames=BCAM0899;
OS   Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS   NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=216591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610;
RX   PubMed=18931103; DOI=10.1128/jb.01230-08;
RA   Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA   Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA   Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA   Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA   Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA   Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT   "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT   cystic fibrosis patients.";
RL   J. Bacteriol. 191:261-277(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; AM747721; CAR54756.1; -; Genomic_DNA.
DR   RefSeq; WP_006486428.1; NC_011001.1.
DR   AlphaFoldDB; B4EN17; -.
DR   SMR; B4EN17; -.
DR   STRING; 216591.BCAM0899; -.
DR   EnsemblBacteria; CAR54756; CAR54756; BCAM0899.
DR   GeneID; 56561541; -.
DR   KEGG; bcj:BCAM0899; -.
DR   eggNOG; COG2334; Bacteria.
DR   HOGENOM; CLU_053300_0_0_4; -.
DR   OMA; DPTHFER; -.
DR   OrthoDB; 1003984at2; -.
DR   BioCyc; BCEN216591:G1G1V-4882-MON; -.
DR   UniPathway; UPA00050; UER00064.
DR   Proteomes; UP000001035; 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_1000115427"
SQ   SEQUENCE   332 AA;  37189 MW;  78ED8622AD75E577 CRC64;
     MAVFTAVSDS DLAQWMRHYE LGDVLAFRGI PSGIENSNFF LTTTRGEYVL TIFEKLTAQQ
     LPFYLDLMRH LAAHGVPVPD PIPRDDGALF GELHGKPAAI VTKLDGAAEL APGVEHCIEV
     GQMLARLHLA GRDYPRSQPN LRSLPWWQEN VPAIVPFITD AQRTLLEGEL AHQAGFFASD
     DYAALPAGPC HCDLFRDNVL FAHAAPGTGH DVRLGGFFDF YFAGCDKWLF DVAVTVNDWC
     VDLATGVLDV ARADALLRAY QTVRPFTAEE RRHWSDMLRA GAYRFWVSRL YDFYLPRAAE
     MLKPHDPGHF ERILRERIAH TPALPEIQTA CN