ID   KHSE_BURMS              Reviewed;         331 AA.
AC   A1UYM9;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 69.
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=BMASAVP1_1486;
OS   Burkholderia mallei (strain SAVP1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320388;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAVP1;
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=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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABM49441.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000525; ABM49441.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_004190439.1; NC_008784.1.
DR   AlphaFoldDB; A1UYM9; -.
DR   SMR; A1UYM9; -.
DR   GeneID; 56598211; -.
DR   KEGG; bmv:BMASAVP1_1486; -.
DR   HOGENOM; CLU_053300_0_0_4; -.
DR   UniPathway; UPA00050; UER00064.
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..331
FT                   /note="Homoserine kinase"
FT                   /id="PRO_0000322238"
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