ID   KHSE_GRABC              Reviewed;         319 AA.
AC   Q0BQX8;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=GbCGDNIH1_1876;
OS   Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Granulibacter.
OX   NCBI_TaxID=391165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1260 / CGDNIH1;
RX   PubMed=17827295; DOI=10.1128/jb.00793-07;
RA   Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA   Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT   "Genome sequence analysis of the emerging human pathogenic acetic acid
RT   bacterium Granulibacter bethesdensis.";
RL   J. Bacteriol. 189:8727-8736(2007).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000394; ABI62774.1; -; Genomic_DNA.
DR   RefSeq; WP_011632576.1; NC_008343.2.
DR   AlphaFoldDB; Q0BQX8; -.
DR   SMR; Q0BQX8; -.
DR   STRING; 391165.GbCGDNIH1_1876; -.
DR   EnsemblBacteria; ABI62774; ABI62774; GbCGDNIH1_1876.
DR   KEGG; gbe:GbCGDNIH1_1876; -.
DR   eggNOG; COG2334; Bacteria.
DR   HOGENOM; CLU_053300_1_0_5; -.
DR   OMA; DPTHFER; -.
DR   UniPathway; UPA00050; UER00064.
DR   Proteomes; UP000001963; 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..319
FT                   /note="Homoserine kinase"
FT                   /id="PRO_0000300792"
SQ   SEQUENCE   319 AA;  34916 MW;  9BD467252903CBA5 CRC64;
     MAVYTEVTDE ALAAFLAEYD IGTAVAFRGI AEGVENSNYV LRTTGGDYIL TLYEKRVDPN
     DLPWFLGLME HLAARGITCP QPVRGRDGQA LRMLCGRHAA ITGFLPGVWP RKVQVAHCHP
     VGEVLAKLHE AGADYAPTRL NALGPEGWPP LLAICRSRAD EISPGLGEEL QKALDRVLTA
     WPSDLPAGHI HADLFPDNVF FLDDRLSGVI DFYFAATDAL AYDIAIALNA WCFESDHAYN
     ITKGSALLRG YNAIRTLTEA EKAALPVLCQ GAALRFALTR LFDWLNTPPG AMVTRKDPMD
     YVHRLRFHLS APNAGAYGL