ID   KHSE_SINFN              Reviewed;         326 AA.
AC   C3MHK2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=NGR_c05340;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/aem.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT   systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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; CP001389; ACP24330.1; -; Genomic_DNA.
DR   RefSeq; WP_012707115.1; NC_012587.1.
DR   RefSeq; YP_002825083.1; NC_012587.1.
DR   AlphaFoldDB; C3MHK2; -.
DR   SMR; C3MHK2; -.
DR   STRING; 394.NGR_c05340; -.
DR   EnsemblBacteria; ACP24330; ACP24330; NGR_c05340.
DR   KEGG; rhi:NGR_c05340; -.
DR   PATRIC; fig|394.7.peg.3347; -.
DR   eggNOG; COG2334; Bacteria.
DR   HOGENOM; CLU_053300_1_0_5; -.
DR   OMA; DPTHFER; -.
DR   OrthoDB; 1003984at2; -.
DR   UniPathway; UPA00050; UER00064.
DR   Proteomes; UP000001054; 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..326
FT                   /note="Homoserine kinase"
FT                   /id="PRO_1000196947"
SQ   SEQUENCE   326 AA;  36234 MW;  D09C94CF3805D565 CRC64;
     MAVYTDITED ELAGFLAAYD VGTLTSYKGI AEGVENSNFL LHTTRGSYIL TLYEKRVNAD
     DLPFFLGLMH HLAERGLSCP LPLPRADGAL LGTLSGRPAA VISFLEGMWL RKPEAQHCRE
     VGRALASMHE AGEGFALTRA NALSVGGWRP LWRNSEARAD EVQDGLKEDI AAELAYLEDH
     WPRNLPQGVI HADLFPDNVF FLGDRLSGLI DFYFACNDFL AYDIAVCLNS WCFEKNGSYN
     ITKGMALLSG YESVRKLTAE EVSALPLLAR GSALRFFLTR LYDWLMTPAG ALVVKKDPLE
     YLTKLRFHRA VVSSAEYGLR RDEASQ