ID   D5VTF3_METIM            Unreviewed;       290 AA.
AC   D5VTF3;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=Homoserine kinase {ECO:0000256|ARBA:ARBA00012078, 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   OrderedLocusNames=Metin_1203 {ECO:0000313|EMBL:ADG13856.1};
OS   Methanocaldococcus infernus (strain DSM 11812 / JCM 15783 / ME).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=573063 {ECO:0000313|EMBL:ADG13856.1, ECO:0000313|Proteomes:UP000002061};
RN   [1] {ECO:0000313|EMBL:ADG13856.1, ECO:0000313|Proteomes:UP000002061}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11812 / JCM 15783 / ME {ECO:0000313|Proteomes:UP000002061};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Woyke T.;
RT   "Complete sequence of Methanocaldococcus infernus ME.";
RL   Submitted (APR-2010) 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|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}.
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DR   EMBL; CP002009; ADG13856.1; -; Genomic_DNA.
DR   RefSeq; WP_013100601.1; NC_014122.1.
DR   AlphaFoldDB; D5VTF3; -.
DR   STRING; 573063.Metin_1203; -.
DR   GeneID; 9132222; -.
DR   KEGG; mif:Metin_1203; -.
DR   eggNOG; arCOG01027; Archaea.
DR   HOGENOM; CLU_041243_1_1_2; -.
DR   OrthoDB; 28273at2157; -.
DR   UniPathway; UPA00050; UER00064.
DR   Proteomes; UP000002061; 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   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   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          73..140
FT                   /note="GHMP kinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00288"
FT   DOMAIN          197..274
FT                   /note="GHMP kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08544"
FT   BINDING         81..91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00384"
SQ   SEQUENCE   290 AA;  31739 MW;  6CBC63B3ABC7C485 CRC64;
     MKVKAPCSSA NLGVGFDVFG LCLEEPYDII EVKKIDEGIE IEGKDIPLNP KENVAGVVAE
     KMLKDFNIES GVKIKIKKGI KGGSGLGSSA ASAAGTAFAI NELFNLKLSK LKLVDYASYG
     ELIASGAKHA DNVAPAIYGG FTIVNYNPLN VLHIDVDFNV IVAIPNVKIE TKKAREIIPK
     EVSLKDMVHN LGRATGMIYA LFNNDLELFG KYMMEDKIVE PYRGKLIPHY FEVKEKLKNL
     AYGVCISGSG PSILVIPKEE FQDEIIDILS SYYDKIIKTR VGKGCELYKA
//