ID   KHSE_BURP6              Reviewed;         331 AA.
AC   A3NMH8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 84.
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=BURPS668_A2556;
OS   Burkholderia pseudomallei (strain 668).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=668;
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}.
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DR   EMBL; CP000571; ABN87275.1; -; Genomic_DNA.
DR   RefSeq; WP_011853655.1; NC_009075.1.
DR   AlphaFoldDB; A3NMH8; -.
DR   SMR; A3NMH8; -.
DR   KEGG; bpd:BURPS668_A2556; -.
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   Gene3D; 3.90.1200.10; -; 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   NCBIfam; TIGR00938; thrB_alt; 1.
DR   PANTHER; PTHR21064:SF6; APH DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR21064; UNCHARACTERIZED; 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_1000022579"
SQ   SEQUENCE   331 AA;  36766 MW;  347290E49DEC192C CRC64;
     MAVFTAVSDA DLALWMRHYD LGDVVAFRGI PSGIENSNFF LTTTRGEYVL TIFENLTAGQ
     LPFYVHLMSH LAKHGVPVPA PVARDDGTLF GELHGKPAAI VTKLEGAAQL APGVEHCVEV
     GQMLARMHLA GRDYPRHQPN LRSLPWWRDT VPAIAPFVTG EQRALLEGEL AHQAAFFASD
     DYAALPEGPC HCDLFRDNAL FAHAEPDTGH SVRLGGFFDF YFAGCDKWLF DVAVTVNDWC
     VDLPTGALDA ARADALLRAY QTVRPFTAGE RRHWGDMLRA GAYRFWVSRL YDFHLPRAAQ
     MLKPHDPGHF ERILRERIAH AGAPPETHAC N
//