ID KHSE_PYRCJ Reviewed; 296 AA. AC A3MT44; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, sequence version 1. DT 16-MAY-2012, entry version 41. DE RecName: Full=Homoserine kinase; DE Short=HK; DE Short=HSK; DE EC=2.7.1.39; GN Name=thrB; OrderedLocusNames=Pcal_0376; OS Pyrobaculum calidifontis (strain JCM 11548 / VA1). OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; OC Thermoproteaceae; Pyrobaculum. OX NCBI_TaxID=410359; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 11548 / VA1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Cozen A.E., Fitz-Gibbon S.T., House C.H., Saltikov C., RA Lowe T.M., Richardson P.; RT "Complete sequence of Pyrobaculum calidifontis JCM 11548."; RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of L- CC homoserine to L-homoserine phosphate (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + L-homoserine = ADP + O-phospho-L- CC homoserine. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 4/5. CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). CC -!- SIMILARITY: Belongs to the GHMP kinase family. Homoserine kinase CC subfamily. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000561; ABO07811.1; -; Genomic_DNA. DR RefSeq; YP_001055277.1; NC_009073.1. DR ProteinModelPortal; A3MT44; -. DR STRING; A3MT44; -. DR GeneID; 4908224; -. DR GenomeReviews; CP000561_GR; Pcal_0376. DR KEGG; pcl:Pcal_0376; -. DR eggNOG; COG0083; -. DR HOGENOM; HOG000247197; -. DR KO; K00872; -. DR OMA; IPGYDNA; -. DR ProtClustDB; CLSK631101; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004413; F:homoserine kinase activity; IEA:EC. DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; G3DSA:3.30.230.10; Ribosomal_S5_D2-type_fold; 1. DR HAMAP; MF_00384; Homoser_kinase; 1; -. DR InterPro; IPR013750; GHMP_kinase_C_dom. 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 PRINTS; PR00958; HOMSERKINASE. DR SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 1. DR PROSITE; PS00627; GHMP_KINASES_ATP; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm; KW Kinase; Nucleotide-binding; Threonine biosynthesis; Transferase. FT CHAIN 1 296 Homoserine kinase. FT /FTId=PRO_1000122434. FT NP_BIND 79 89 ATP (Potential). SQ SEQUENCE 296 AA; 30486 MW; 3F4E620A332F1624 CRC64; MRAPSTSANL GAGFDVVAVA HDAYFAEAYV AVEQGCGVAV KFKGYDPGEN NTVSLAFRHL FNMLGICRQV EVVVDNRIPL ARGLGSSGAS AVAALAAFIR EAGLKAEPKL VVEAAGLGEV AAAGSPHFDN VAGAALGGAV VVVSTSPLEV VKFSPKLLFV VGVPDVPPIP EKTRLMRSVL PREVPFKTYV AQLARVSALV AGFATSNPRL VALGMSDDVV EPARAPYVHG YARARRYALE AGALGFAISG AGPSVVALVD DKHSDAVRAA LARAYAEEGL RAEVKVAQVA EGALGV //