ID   KHSE_BURM7              Reviewed;         331 AA.
AC   A3MBA7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   04-NOV-2026, entry version 91.
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=BMA10247_A0338;
OS   Burkholderia mallei (strain NCTC 10247).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320389;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 10247;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-homoserine + ATP = O-phospho-L-homoserine + ADP + H(+);
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; CP000547; ABO02781.1; -; Genomic_DNA.
DR   RefSeq; WP_004190439.1; NC_009079.1.
DR   AlphaFoldDB; A3MBA7; -.
DR   SMR; A3MBA7; -.
DR   GeneID; 92976997; -.
DR   KEGG; bmn:BMA10247_A0338; -.
DR   OMA; AACRFWS; -.
DR   UniPathway; UPA00050; UER00064.
DR   GO; GO:0004413; F:homoserine kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009088; P:L-threonine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd05153; HomoserineK_II; 1.
DR   Gene3D; 3.90.1200.10; -; 1.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 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   InterPro; IPR050249; Pseudomonas-type_ThrB.
DR   NCBIfam; NF003558; PRK05231.1; 1.
DR   NCBIfam; TIGR00938; thrB_alt; 1.
DR   PANTHER; PTHR21064:SF6; AMINOGLYCOSIDE PHOSPHOTRANSFERASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR21064; AMINOGLYCOSIDE PHOSPHOTRANSFERASE DOMAIN-CONTAINING PROTEIN-RELATED; 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..331
FT                   /note="Homoserine kinase"
FT                   /id="PRO_1000022577"
SQ   SEQUENCE   331 AA;  36779 MW;  587176329DF0897C CRC64;
     MAVFTAVSDA DLALWMRHYD LGDVVAFRGI PSGIENSNFF LTTTRGEYVL TIFENLTAGQ
     LPFYVDLMSH LAKHGVPVPA PVARDDGTLF GELHGKPAAI VTKLEGAAQL APGVEHCVEV
     GQMLARMHLA GRDYPRHQPN LRSLPWWRDT VPAIAPFVTG EQRALLEGEL AHQAAFFASD
     DYAALPEGPC HCDLFRDNAL FAHAEPDTGH SVRLGGFFDF YFAGCDKWLF DVAVTVNDWC
     VDLPTGALDA ARADALLRAY QTVRPFTAGE RRRWGDMLRA GAYRFWVSRL YDFHLPRAAQ
     MLKPHDPGHF ERILRERIAH AGALPETHAC N
//