ID   KHSE_PHEZH              Reviewed;         323 AA.
AC   B4R8T4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
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}; OrderedLocusNames=PHZ_c2890;
OS   Phenylobacterium zucineum (strain HLK1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Phenylobacterium.
OX   NCBI_TaxID=450851;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLK1;
RX   PubMed=18700039; DOI=10.1186/1471-2164-9-386;
RA   Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.;
RT   "Complete genome of Phenylobacterium zucineum - a novel facultative
RT   intracellular bacterium isolated from human erythroleukemia cell line
RT   K562.";
RL   BMC Genomics 9:386-386(2008).
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; CP000747; ACG79299.1; -; Genomic_DNA.
DR   RefSeq; WP_012523437.1; NC_011144.1.
DR   AlphaFoldDB; B4R8T4; -.
DR   SMR; B4R8T4; -.
DR   STRING; 450851.PHZ_c2890; -.
DR   PRIDE; B4R8T4; -.
DR   EnsemblBacteria; ACG79299; ACG79299; PHZ_c2890.
DR   KEGG; pzu:PHZ_c2890; -.
DR   eggNOG; COG2334; Bacteria.
DR   HOGENOM; CLU_053300_1_0_5; -.
DR   OMA; DPTHFER; -.
DR   OrthoDB; 1003984at2; -.
DR   UniPathway; UPA00050; UER00064.
DR   Proteomes; UP000001868; 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   Reference proteome; Threonine biosynthesis; Transferase.
FT   CHAIN           1..323
FT                   /note="Homoserine kinase"
FT                   /id="PRO_1000115437"
SQ   SEQUENCE   323 AA;  35333 MW;  0F87BBA2DE8E3547 CRC64;
     MAVYTDITDD ELAKLLADFD LGAPLSFKGI AEGVENSNFL LETEGGRFIL TVYEKRVRAE
     DLPFFLGLMR WLSEHGFASG LPMADRGGEM LKTVRGKPCA IVSFLPGLSV RRPTVAHCRE
     AGKGLAALHN AADGFPMRRE NDLGQGAWAP MFERLKDDAE RLKPGLAEVI ARDVADLADR
     WPQGLPEGVI HADYFPDNVF FKEGVFAGAI DFYFACNDIR AYDIAVALNA WCFEADGSFN
     ITAARALVAG YEAVRPLSEA ERAALPVLAH GAALRFFLTR LHDWHATPAG ALVKPKDPLE
     YERKLAVHRT SPDLVLFGAA AAE