KHSE_STRPN
ID KHSE_STRPN Reviewed; 289 AA.
AC P0A3L7; P72535;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Homoserine kinase;
DE Short=HK;
DE Short=HSK;
DE EC=2.7.1.39;
GN Name=thrB; OrderedLocusNames=SP_1360;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(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}.
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DR EMBL; AE005672; AAK75458.1; -; Genomic_DNA.
DR PIR; A95158; A95158.
DR RefSeq; WP_000692438.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; P0A3L7; -.
DR SMR; P0A3L7; -.
DR STRING; 170187.SP_1360; -.
DR EnsemblBacteria; AAK75458; AAK75458; SP_1360.
DR GeneID; 60233312; -.
DR GeneID; 66806477; -.
DR KEGG; spn:SP_1360; -.
DR eggNOG; COG0083; Bacteria.
DR OMA; CANRIPH; -.
DR PhylomeDB; P0A3L7; -.
DR BioCyc; SPNE170187:G1FZB-1368-MON; -.
DR UniPathway; UPA00050; UER00064.
DR Proteomes; UP000000585; 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..289
FT /note="Homoserine kinase"
FT /id="PRO_0000156619"
FT BINDING 79..89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 289 AA; 31548 MW; BA1BBA895A72BD18 CRC64;
MKIIVPATSA NIGPGFDSVG VAVTKYLQIE VCEERDEWLI EHQIGKWIPH DERNLLLKIA
LQIVPDLQPR RLKMTSDVPL ARGLGSSSSV IVAGIELANQ LGQLNLSDHE KLQLATKIEG
HPDNVAPAIY GNLVIASSVE GQVSAIVADF PECDFLAYIP NYELRTRDSR SVLPKKLSYK
EAVAASSIAN VAVAALLAGD MVTAGQAIEG DLFHERYRQD LVREFAMIKQ VTKENGAYAT
YLSGAGPTVM VLASHDKMPT IKAELEKQPF KGKLHDLRVD TQGVRVEAK