ID   KHSE_NEIMA              Reviewed;         305 AA.
AC   Q9JWE5; A1IPM8;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   03-AUG-2022, entry version 104.
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=NMA0411;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA   Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA   Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT   Z2491.";
RL   Nature 404:502-506(2000).
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   -!- SEQUENCE CAUTION:
CC       Sequence=CAM07699.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL157959; CAM07699.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_002247181.1; NC_003116.1.
DR   AlphaFoldDB; Q9JWE5; -.
DR   SMR; Q9JWE5; -.
DR   EnsemblBacteria; CAM07699; CAM07699; NMA0411.
DR   KEGG; nma:NMA0411; -.
DR   HOGENOM; CLU_053300_0_0_4; -.
DR   BioCyc; NMEN122587:NMA_RS02075-MON; -.
DR   UniPathway; UPA00050; UER00064.
DR   Proteomes; UP000000626; 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..305
FT                   /note="Homoserine kinase"
FT                   /id="PRO_0000172192"
SQ   SEQUENCE   305 AA;  33657 MW;  2A3C7086F3257EFD CRC64;
     MSVYTSVSDD EMRGFLSGYD LGEFVSLQGI AQGITNSNYF LTTTSGRYVL TVFEVLKQEE
     LPFFLELNRH LSMKGVAVAA PVARKDGRLD SVLAGKPACL VACLKGSDTA LPTAEQCFHT
     GAMLAKMHLA AADFPLEMEN PRYDAWWTEA CARLLPVLSQ DDAALLRAEI DALKDNLGNH
     LPSGIIHADL FKDNVLLDGG QVSGFIDFYY ACRGNFMYDL AIAVNDWART ADNKLDEALK
     KAFIGGYEGV RPLSAEEKAY FPTAQRAGCI RFWVSRLLDF HFPQAGEMTF IKDPNAFRNL
     LLSLG