ID   KHSE_PSEAB              Reviewed;         316 AA.
AC   Q02DL4;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=PA14_72510;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA   Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
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; CP000438; ABJ14881.1; -; Genomic_DNA.
DR   RefSeq; WP_003110565.1; NZ_CP034244.1.
DR   AlphaFoldDB; Q02DL4; -.
DR   SMR; Q02DL4; -.
DR   EnsemblBacteria; ABJ14881; ABJ14881; PA14_72510.
DR   KEGG; pau:PA14_72510; -.
DR   HOGENOM; CLU_053300_0_0_6; -.
DR   OMA; DPTHFER; -.
DR   BioCyc; PAER208963:G1G74-6101-MON; -.
DR   UniPathway; UPA00050; UER00064.
DR   Proteomes; UP000000653; Chromosome.
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..316
FT                   /note="Homoserine kinase"
FT                   /id="PRO_0000300797"
SQ   SEQUENCE   316 AA;  35362 MW;  265BC7B1F4EACBD3 CRC64;
     MSVFTPLERS TLEAFLAPYD LGRLRDFRGI AEGSENSNFF VSLEHGEFVL TLVERGPVQD
     LPFFIELLDV LHEDGLPVPY ALRTRDGEAL RRLEGKPALL QPRLAGRHER QPNAHHCQEV
     GDLLGHLHAA TRGRILERPS DRGLPWMLEQ GANLAPRLPE QARALLAPAL AEIAALDAER
     PALPRANLHA DLFRDNVLFD GPHLAGLIDF YNACSGWMLY DLAITLNDWC SNADGSLDPA
     RARALLAAYA NRRPFTALEA EHWPSMLRVA CVRFWLSRLI AAEAFAGQDV LIHDPAEFEM
     RLAQRQNVEI HLPFAL