KHSE_ALKCK
ID KHSE_ALKCK Reviewed; 297 AA.
AC Q5WDT6;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=ABC2940;
OS Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=66692;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSM-K16;
RA Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA Kawai S., Ito S., Horikoshi K.;
RT "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT K16.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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; AP006627; BAD65474.1; -; Genomic_DNA.
DR RefSeq; WP_011247782.1; NC_006582.1.
DR AlphaFoldDB; Q5WDT6; -.
DR SMR; Q5WDT6; -.
DR STRING; 66692.ABC2940; -.
DR EnsemblBacteria; BAD65474; BAD65474; ABC2940.
DR KEGG; bcl:ABC2940; -.
DR eggNOG; COG0083; Bacteria.
DR HOGENOM; CLU_041243_0_0_9; -.
DR OMA; CANRIPH; -.
DR OrthoDB; 610857at2; -.
DR UniPathway; UPA00050; UER00064.
DR Proteomes; UP000001168; 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; 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.
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..297
FT /note="Homoserine kinase"
FT /id="PRO_0000156553"
FT BINDING 84..94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00384"
SQ SEQUENCE 297 AA; 31324 MW; 9546BD9B1A66C60B CRC64;
MAFSITVPAS TANLGPGFDS IGLALNRYLH LEVEQASKWS FICSSPGLEN IGTDNLVTKA
ATFASKEWGK VLPPCQVVMK NDIPLSKGFG SSAAAIVAGI ELAASVCGQF ASKAEKARLA
SLWEGHPDNV AASIYGGLVI GTHSEESTEI LHVEAPNIDL VALIPSKTLA TKKARAVLPD
MLSYKEAVQA SSVANVLAAA LVKQDWELVG KMMLADRFHQ PYRQQLIPHL PDVCAYAQAD
EDAYGAALSG AGPIILCLVK EGKGEAFASR LHKQFPACRA EVMRPAVQGS AVSIAQA
