ID A0A481QAT8_9GAMM Unreviewed; 309 AA. AC A0A481QAT8; DT 05-JUN-2019, integrated into UniProtKB/TrEMBL. DT 05-JUN-2019, sequence version 1. DT 03-MAY-2023, entry version 15. DE RecName: Full=Homoserine kinase {ECO:0000256|ARBA:ARBA00017858, ECO:0000256|HAMAP-Rule:MF_00384}; DE Short=HK {ECO:0000256|HAMAP-Rule:MF_00384}; DE Short=HSK {ECO:0000256|HAMAP-Rule:MF_00384}; DE EC=2.7.1.39 {ECO:0000256|ARBA:ARBA00012078, ECO:0000256|HAMAP-Rule:MF_00384}; GN Name=thrB {ECO:0000256|HAMAP-Rule:MF_00384}; GN ORFNames=D5F51_03595 {ECO:0000313|EMBL:QAX77710.1}; OS Yersinia hibernica. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Yersinia. OX NCBI_TaxID=2339259 {ECO:0000313|EMBL:QAX77710.1, ECO:0000313|Proteomes:UP000288804}; RN [1] {ECO:0000313|Proteomes:UP000288804} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CFS1934 {ECO:0000313|Proteomes:UP000288804}; RA Nguyen S.V., Mundanda D.M., Anes J., Fanning S.; RT "Yersinia hibernicus sp. nov."; RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of L-homoserine CC to L-homoserine phosphate. {ECO:0000256|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:0000256|ARBA:ARBA00000528, CC ECO:0000256|HAMAP-Rule:MF_00384}; CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine CC from L-aspartate: step 4/5. {ECO:0000256|ARBA:ARBA00005015, CC ECO:0000256|HAMAP-Rule:MF_00384}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00384}. CC -!- SIMILARITY: Belongs to the GHMP kinase family. Homoserine kinase CC subfamily. {ECO:0000256|ARBA:ARBA00007370, ECO:0000256|HAMAP- CC 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; CP032487; QAX77710.1; -; Genomic_DNA. DR AlphaFoldDB; A0A481QAT8; -. DR EnsemblBacteria; QAX77710; QAX77710; D5F51_03595. DR KEGG; yhi:D5F51_03595; -. DR OrthoDB; 9769912at2; -. DR UniPathway; UPA00050; UER00064. DR Proteomes; UP000288804; 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; GHMP kinase, C-terminal domain; 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 PANTHER; PTHR20861:SF1; HOMOSERINE KINASE; 1. DR PANTHER; PTHR20861; HOMOSERINE/4-DIPHOSPHOCYTIDYL-2-C-METHYL-D-ERYTHRITOL KINASE; 1. 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; SSF55060; GHMP Kinase, C-terminal domain; 1. DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1. DR TIGRFAMs; TIGR00191; thrB; 1. DR PROSITE; PS00627; GHMP_KINASES_ATP; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00384}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00384}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00384}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00384}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00384}; KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697, ECO:0000256|HAMAP- KW Rule:MF_00384}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00384}. FT DOMAIN 85..150 FT /note="GHMP kinase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00288" FT DOMAIN 212..286 FT /note="GHMP kinase C-terminal" FT /evidence="ECO:0000259|Pfam:PF08544" FT BINDING 91..101 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00384" SQ SEQUENCE 309 AA; 33132 MW; E3DB4BA6AF6E6790 CRC64; MVKVYAPASI GNVSVGFDVL GAAVSPLDGT LLGDCVSVTA ADSFSLRNEG RFVSKLPDDP KENIVYQCWA RFCQEMGKEI PVAMVLEKNM PIGSGLGSSA CSVVAGLMAM NEFCGKPLDK VTLLGMMGEL EGRVSGSVHF DNVAPCYLGG MQLILEQPGY ISQNVPGFDD WLWVMAYPGI KVSTAEARAI LPAQYRRQDC IAHGRNVAGF IHACHTQQPD LAAKMMKDVI AEPYRTQLLP GFAAARQAAL DIGALACGIS GSGPTLFAVC NEIETAQRMA NWLQNHYLQN DEGFVHICRL DTAGARLLG //