KHSE_STAAE
ID KHSE_STAAE Reviewed; 304 AA.
AC A6QGN2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Homoserine kinase {ECO:0000255|HAMAP-Rule:MF_00384};
DE Short=HK {ECO:0000255|HAMAP-Rule:MF_00384};
DE Short=HSK {ECO:0000255|HAMAP-Rule:MF_00384};
DE EC=2.7.1.39 {ECO:0000255|HAMAP-Rule:MF_00384};
GN Name=thrB {ECO:0000255|HAMAP-Rule:MF_00384}; OrderedLocusNames=NWMN_1242;
OS Staphylococcus aureus (strain Newman).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=426430;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Newman;
RX PubMed=17951380; DOI=10.1128/jb.01000-07;
RA Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT analysis of staphylococcal genomes: polymorphism and evolution of two major
RT pathogenicity islands.";
RL J. Bacteriol. 190:300-310(2008).
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of L-homoserine
CC to L-homoserine phosphate. {ECO:0000255|HAMAP-Rule:MF_00384}.
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_00384};
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00384}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00384}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. Homoserine kinase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00384}.
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DR EMBL; AP009351; BAF67514.1; -; Genomic_DNA.
DR RefSeq; WP_000073184.1; NZ_CP023390.1.
DR AlphaFoldDB; A6QGN2; -.
DR SMR; A6QGN2; -.
DR EnsemblBacteria; BAF67514; BAF67514; NWMN_1242.
DR KEGG; sae:NWMN_1242; -.
DR HOGENOM; CLU_041243_0_0_9; -.
DR OMA; CANRIPH; -.
DR UniPathway; UPA00050; UER00064.
DR Proteomes; UP000006386; 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; -; 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_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR Pfam; PF08544; GHMP_kinases_C; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR PIRSF; PIRSF000676; Homoser_kin; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55060; SSF55060; 1.
DR TIGRFAMs; TIGR00191; thrB; 1.
DR PROSITE; PS00627; GHMP_KINASES_ATP; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; ATP-binding; Cytoplasm; Kinase;
KW Nucleotide-binding; Threonine biosynthesis; Transferase.
FT CHAIN 1..304
FT /note="Homoserine kinase"
FT /id="PRO_1000072189"
FT BINDING 90..100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00384"
SQ SEQUENCE 304 AA; 33267 MW; BB6FACEF01A3C0E9 CRC64;
MSNVLELTIP ASTANLGVGF DSIGMALDKF LHLSVKETSG TKWEYIFHDD ASKQLPTDET
NFIYHVAQQV ASKYSVDLPN LCIEMRSDIP LARGLGSSAS ALVGAIYIAN YFGDIQLSKH
EVLQLATEIE GHPDNVAPTI YGGLIAGYYN DVSKETSVAH IDIPDVDVIV TIPTYELKTE
ASRRALPQKL THSEAVKSSA ISNTMICALA QHNYELAGKL MQQDGFHEPY RQHLIAEFDE
VKTIASQHNA YATVISGAGP TILIFSRKEN SGELVRSLNS QVVSCHSELV DINISGVKER
IVYQ