ID KHSE_PROM0 Reviewed; 315 AA. AC A3PBW9; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, sequence version 1. DT 02-NOV-2016, entry version 66. 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}; GN OrderedLocusNames=P9301_06211; OS Prochlorococcus marinus (strain MIT 9301). OC Bacteria; Cyanobacteria; Synechococcales; Prochloraceae; OC Prochlorococcus. OX NCBI_TaxID=167546; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MIT 9301; RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231; RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., RA Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., RA Steglich C., Church G.M., Richardson P., Chisholm S.W.; RT "Patterns and implications of gene gain and loss in the evolution of RT Prochlorococcus."; RL PLoS Genet. 3:2515-2528(2007). CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of L- CC homoserine to L-homoserine phosphate. {ECO:0000255|HAMAP- CC Rule:MF_00384}. CC -!- CATALYTIC ACTIVITY: ATP + L-homoserine = ADP + O-phospho-L- CC homoserine. {ECO:0000255|HAMAP-Rule:MF_00384}. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 4/5. {ECO:0000255|HAMAP- CC 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}. 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; CP000576; ABO17244.1; -; Genomic_DNA. DR RefSeq; WP_011862611.1; NC_009091.1. DR ProteinModelPortal; A3PBW9; -. DR STRING; 167546.P9301_06211; -. DR EnsemblBacteria; ABO17244; ABO17244; P9301_06211. DR KEGG; pmg:P9301_06211; -. DR PATRIC; 22994837; VBIProMar103344_0607. DR eggNOG; ENOG4105D5I; Bacteria. DR eggNOG; COG0083; LUCA. DR HOGENOM; HOG000247199; -. DR KO; K00872; -. DR OMA; CANRIPH; -. DR OrthoDB; POG091H020X; -. DR UniPathway; UPA00050; UER00064. DR Proteomes; UP000001430; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004413; F:homoserine kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-HAMAP. 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; 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; Complete proteome; Cytoplasm; KW Kinase; Nucleotide-binding; Threonine biosynthesis; Transferase. FT CHAIN 1 315 Homoserine kinase. FT /FTId=PRO_1000049155. FT NP_BIND 97 107 ATP. {ECO:0000255|HAMAP-Rule:MF_00384}. SQ SEQUENCE 315 AA; 33579 MW; A02F0A10DEF2DC99 CRC64; MSIPEVGKKI RVTVPSTTAN LGPGFDCLGA ALDLYNEFIF TRIEGGGDRF DLIMESTDGN HLRGGPENLV FRAAQKVWES ANMDPFALEA RVKLAVPPAR GLGSSATAIV AGLIGANAIM NSPLSKEKLL ELAIDIEGHP DNVVPSLLGG LCLTARSSSQ RWRIIRCEWH YSIKAVVAIP AIRLSTSEAR KVMPRNVPIS DAVTNMGALT LLLNGLKTGN EELIKEGMFD KLHEPYRWKL IKGGLEVKDA ALNAGALGCA ISGAGPSILA LCKKENGKNV SQAMVKAWEM SGVASRAPFL NVQTTGSQFS TISGK //