ID KHSE_METJA Reviewed; 296 AA. AC Q58504; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 2. DT 27-MAR-2024, entry version 146. DE RecName: Full=Homoserine kinase; DE Short=HK; DE Short=HSK; DE EC=2.7.1.39; GN Name=thrB; OrderedLocusNames=MJ1104; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM OS 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L., RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). RX PubMed=11188689; DOI=10.1016/s0969-2126(00)00533-5; RA Zhou T., Daugherty M., Grishin N.V., Osterman A.L., Zhang H.; RT "Structure and mechanism of homoserine kinase: prototype for the GHMP RT kinase superfamily."; RL Structure 8:1247-1257(2000). 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}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99107.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; L77117; AAB99107.1; ALT_INIT; Genomic_DNA. DR PIR; G64437; G64437. DR RefSeq; WP_064496725.1; NC_000909.1. DR PDB; 1FWK; X-ray; 2.10 A; A/B/C/D=1-296. DR PDB; 1FWL; X-ray; 2.25 A; A/B/C/D=1-296. DR PDB; 1H72; X-ray; 1.80 A; C=1-296. DR PDB; 1H73; X-ray; 2.00 A; A=1-296. DR PDB; 1H74; X-ray; 1.90 A; A/B/C/D=1-296. DR PDBsum; 1FWK; -. DR PDBsum; 1FWL; -. DR PDBsum; 1H72; -. DR PDBsum; 1H73; -. DR PDBsum; 1H74; -. DR AlphaFoldDB; Q58504; -. DR SMR; Q58504; -. DR STRING; 243232.MJ_1104; -. DR PaxDb; 243232-MJ_1104; -. DR EnsemblBacteria; AAB99107; AAB99107; MJ_1104. DR GeneID; 1452001; -. DR KEGG; mja:MJ_1104; -. DR eggNOG; arCOG01027; Archaea. DR HOGENOM; CLU_041243_1_1_2; -. DR InParanoid; Q58504; -. DR OrthoDB; 28273at2157; -. DR PhylomeDB; Q58504; -. DR BioCyc; MetaCyc:MONOMER-14633; -. DR BRENDA; 2.7.1.39; 3260. DR SABIO-RK; Q58504; -. DR UniPathway; UPA00050; UER00064. DR EvolutionaryTrace; Q58504; -. DR Proteomes; UP000000805; 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_Su5_D2-typ_SF. DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr. DR NCBIfam; TIGR00191; thrB; 1. 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 PROSITE; PS00627; GHMP_KINASES_ATP; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; ATP-binding; Cytoplasm; Kinase; KW Nucleotide-binding; Reference proteome; Threonine biosynthesis; KW Transferase. FT CHAIN 1..296 FT /note="Homoserine kinase" FT /id="PRO_0000156641" FT BINDING 86..96 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT STRAND 2..12 FT /evidence="ECO:0007829|PDB:1H72" FT HELIX 15..17 FT /evidence="ECO:0007829|PDB:1H72" FT TURN 18..20 FT /evidence="ECO:0007829|PDB:1H72" FT STRAND 21..47 FT /evidence="ECO:0007829|PDB:1H72" FT TURN 55..57 FT /evidence="ECO:0007829|PDB:1H72" FT HELIX 59..70 FT /evidence="ECO:0007829|PDB:1H72" FT STRAND 76..82 FT /evidence="ECO:0007829|PDB:1H72" FT STRAND 89..91 FT /evidence="ECO:0007829|PDB:1H72" FT HELIX 93..108 FT /evidence="ECO:0007829|PDB:1H72" FT HELIX 115..130 FT /evidence="ECO:0007829|PDB:1H72" FT HELIX 138..143 FT /evidence="ECO:0007829|PDB:1H72" FT STRAND 145..151 FT /evidence="ECO:0007829|PDB:1H72" FT TURN 152..155 FT /evidence="ECO:0007829|PDB:1H72" FT STRAND 156..160 FT /evidence="ECO:0007829|PDB:1H72" FT STRAND 168..171 FT /evidence="ECO:0007829|PDB:1H72" FT HELIX 179..184 FT /evidence="ECO:0007829|PDB:1H72" FT STRAND 188..191 FT /evidence="ECO:0007829|PDB:1H74" FT HELIX 192..210 FT /evidence="ECO:0007829|PDB:1H72" FT HELIX 214..221 FT /evidence="ECO:0007829|PDB:1H72" FT HELIX 228..232 FT /evidence="ECO:0007829|PDB:1H72" FT HELIX 238..245 FT /evidence="ECO:0007829|PDB:1H72" FT HELIX 246..248 FT /evidence="ECO:0007829|PDB:1H72" FT STRAND 249..254 FT /evidence="ECO:0007829|PDB:1H72" FT STRAND 261..265 FT /evidence="ECO:0007829|PDB:1H72" FT HELIX 267..269 FT /evidence="ECO:0007829|PDB:1H72" FT HELIX 270..280 FT /evidence="ECO:0007829|PDB:1H72" FT STRAND 284..287 FT /evidence="ECO:0007829|PDB:1H72" FT STRAND 293..295 FT /evidence="ECO:0007829|PDB:1H74" SQ SEQUENCE 296 AA; 32259 MW; 49919E68F3834C78 CRC64; MKVRVKAPCT SANLGVGFDV FGLCLKEPYD VIEVEAIDDK EIIIEVDDKN IPTDPDKNVA GIVAKKMIDD FNIGKGVKIT IKKGVKAGSG LGSSAASSAG TAYAINELFK LNLDKLKLVD YASYGELASS GAKHADNVAP AIFGGFTMVT NYEPLEVLHI PIDFKLDILI AIPNISINTK EAREILPKAV GLKDLVNNVG KACGMVYALY NKDKSLFGRY MMSDKVIEPV RGKLIPNYFK IKEEVKDKVY GITISGSGPS IIAFPKEEFI DEVENILRDY YENTIRTEVG KGVEVV //