ID   KHSE_BRUA2              Reviewed;         326 AA.
AC   Q2YMI4;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   27-MAR-2024, entry version 95.
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=BAB1_0502;
OS   Brucella abortus (strain 2308).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
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; AM040264; CAJ10458.1; -; Genomic_DNA.
DR   RefSeq; WP_002963634.1; NZ_KN046823.1.
DR   AlphaFoldDB; Q2YMI4; -.
DR   SMR; Q2YMI4; -.
DR   STRING; 359391.BAB1_0502; -.
DR   GeneID; 3788984; -.
DR   KEGG; bmf:BAB1_0502; -.
DR   PATRIC; fig|359391.11.peg.2540; -.
DR   HOGENOM; CLU_053300_1_0_5; -.
DR   PhylomeDB; Q2YMI4; -.
DR   UniPathway; UPA00050; UER00064.
DR   Proteomes; UP000002719; Chromosome I.
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   Gene3D; 3.90.1200.10; -; 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   NCBIfam; TIGR00938; thrB_alt; 1.
DR   PANTHER; PTHR21064:SF6; APH DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR21064; UNCHARACTERIZED; 1.
DR   Pfam; PF01636; APH; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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_0000300783"
SQ   SEQUENCE   326 AA;  36645 MW;  0503E8758D5F1AFA CRC64;
     MAVYTDINEI ELGAFLRHYD IGTLTSYKGI AEGVENSNYL LHTSSGSFIL TLYEKRTNRE
     DLPFFLGLMQ HLAKRGLECP QPVVRNDGAM IGQLAGRPAA IVTFLEGMWM RRPTVAHCEA
     VGEGLAHMHL AGADFPMRRR NGLTLPDWRP LWNLSRKCAD TVERGLVAET EADLDFLEKN
     WPADLPQGVI HADLFPDNAF FLGDRLSGFI DFYFACTDIL AYDVAVCLNA WCFEKDFSYN
     RTKGAALLRG YTSVRPLSEA EADALLVLAR GAAVRFMLTR LYDWLTVPAG SFVVKKDPME
     YVRRMRFHRQ IESAAEYGLE MQGVAA
//