ID   KHSE_BARHE              Reviewed;         319 AA.
AC   Q6G4C4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=BH04420;
OS   Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS   (Rochalimaea henselae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=283166;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT   of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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; BX897699; CAF27251.1; -; Genomic_DNA.
DR   RefSeq; WP_011180375.1; NZ_LRIJ02000001.1.
DR   AlphaFoldDB; Q6G4C4; -.
DR   SMR; Q6G4C4; -.
DR   STRING; 283166.BH04420; -.
DR   PaxDb; Q6G4C4; -.
DR   PRIDE; Q6G4C4; -.
DR   EnsemblBacteria; CAF27251; CAF27251; BH04420.
DR   GeneID; 64156724; -.
DR   KEGG; bhe:BH04420; -.
DR   eggNOG; COG2334; Bacteria.
DR   OMA; DPTHFER; -.
DR   UniPathway; UPA00050; UER00064.
DR   Proteomes; UP000000421; 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..319
FT                   /note="Homoserine kinase"
FT                   /id="PRO_1000022575"
SQ   SEQUENCE   319 AA;  36728 MW;  C88064B9A3BC0813 CRC64;
     MAVHTDIHPN DLKAFLTRYS IGSLLSYQGI VEGIENSNFM LYTTEGKFIL TLYEQRISKD
     DLPFFCNLMQ HLGRRGVPCP QPVIQNNGMM IGELAGRPAA IITFLEGEWV RQSNIYHCCE
     VGCSLAQLHL AAQDFSLSRR NTLSLVDWKC LWKRCQVRKD PLLREFGKKI DTELAFLEEN
     WPSILPTGII HADLFNDNVF FLNDRLSGII DFYFACNDFW AYDLAICLNA WCFEHDHSYN
     LIKARGLLES YQKIRPLVPL ELNAIVLLAR GAALRFLLTR LYDWFNTPPG SVVVKKDPWE
     YWHKLCFFSN VGSLSELGF