ID   KHSE_BURMA              Reviewed;         331 AA.
AC   Q62DV9;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=BMAA0307;
OS   Burkholderia mallei (strain ATCC 23344).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=243160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23344;
RX   PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA   Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA   Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA   Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA   Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA   Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA   Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT   "Structural flexibility in the Burkholderia mallei genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
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; CP000011; AAU46180.1; -; Genomic_DNA.
DR   RefSeq; WP_004190439.1; NC_006349.2.
DR   RefSeq; YP_105119.1; NC_006349.2.
DR   AlphaFoldDB; Q62DV9; -.
DR   SMR; Q62DV9; -.
DR   STRING; 243160.BMAA0307; -.
DR   EnsemblBacteria; AAU46180; AAU46180; BMAA0307.
DR   GeneID; 56598211; -.
DR   KEGG; bma:BMAA0307; -.
DR   PATRIC; fig|243160.12.peg.3808; -.
DR   eggNOG; COG2334; Bacteria.
DR   HOGENOM; CLU_053300_0_0_4; -.
DR   OMA; DPTHFER; -.
DR   UniPathway; UPA00050; UER00064.
DR   Proteomes; UP000006693; 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..331
FT                   /note="Homoserine kinase"
FT                   /id="PRO_0000300787"
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