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Database: UniProt
Entry: KHSE_NOSS1
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Original site: KHSE_NOSS1 
ID   KHSE_NOSS1              Reviewed;         298 AA.
AC   Q8YZV9;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   26-JUL-2002, sequence version 2.
DT   27-MAR-2024, entry version 116.
DE   RecName: Full=Homoserine kinase;
DE            Short=HK;
DE            Short=HSK;
DE            EC=2.7.1.39;
GN   Name=thrB; OrderedLocusNames=alr0346;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
CC   -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of L-homoserine
CC       to L-homoserine phosphate. {ECO:0000250}.
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;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 4/5.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. Homoserine kinase
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB72304.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000019; BAB72304.1; ALT_INIT; Genomic_DNA.
DR   PIR; AI1849; AI1849.
DR   AlphaFoldDB; Q8YZV9; -.
DR   SMR; Q8YZV9; -.
DR   STRING; 103690.gene:10492354; -.
DR   KEGG; ana:alr0346; -.
DR   eggNOG; COG0083; Bacteria.
DR   UniPathway; UPA00050; UER00064.
DR   Proteomes; UP000002483; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.890; GHMP kinase, C-terminal domain; 1.
DR   HAMAP; MF_00384; Homoser_kinase; 1.
DR   InterPro; IPR013750; GHMP_kinase_C_dom.
DR   InterPro; IPR036554; GHMP_kinase_C_sf.
DR   InterPro; IPR006204; GHMP_kinase_N_dom.
DR   InterPro; IPR006203; GHMP_knse_ATP-bd_CS.
DR   InterPro; IPR000870; Homoserine_kinase.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   NCBIfam; TIGR00191; thrB; 1.
DR   PANTHER; PTHR20861:SF1; HOMOSERINE KINASE; 1.
DR   PANTHER; PTHR20861; HOMOSERINE/4-DIPHOSPHOCYTIDYL-2-C-METHYL-D-ERYTHRITOL KINASE; 1.
DR   Pfam; PF08544; GHMP_kinases_C; 1.
DR   Pfam; PF00288; GHMP_kinases_N; 1.
DR   PIRSF; PIRSF000676; Homoser_kin; 1.
DR   PRINTS; PR00958; HOMSERKINASE.
DR   SUPFAM; SSF55060; GHMP Kinase, C-terminal domain; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS00627; GHMP_KINASES_ATP; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; ATP-binding; Cytoplasm; Kinase;
KW   Nucleotide-binding; Reference proteome; Threonine biosynthesis;
KW   Transferase.
FT   CHAIN           1..298
FT                   /note="Homoserine kinase"
FT                   /id="PRO_0000156545"
FT   BINDING         92..102
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   298 AA;  31045 MW;  1D3924D410009586 CRC64;
     MSVVSSVTVK VPGTTANLGP GFDCIGAALT IYNQFQFTRL EESGLIIQAT GAEAERVPTD
     ESNLIYQAFA KLYQYIDQPA PGVKIEIELG VPLARGLGSS ATAIVAANRL AGEPLSQAQV
     MALAIAIEGH PDNVVPALLG GCRLAATGAS GWEICDVPWH SHIVPVLAIP DFELSTSEAR
     RVLPTEYSRA DAIFNTAHLG LLLRGLETGK GEWLRAALQD KLHQPYRQAL IPGYDAVNTA
     AVAAGAYGMV ISGAGPTLLA LADVSHAAAV EAAMSTAWQE AGITAVVRSL ALDTHGAT
//
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