ID   B4SGC8_PELPB            Unreviewed;       320 AA.
AC   B4SGC8;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   10-JUN-2026, entry version 103.
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   OrderedLocusNames=Ppha_2706 {ECO:0000313|EMBL:ACF44864.1};
OS   Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1).
OC   Bacteria; Pseudomonadati; Chlorobiota; Chlorobiia; Chlorobiales;
OC   Chlorobiaceae; Chlorobium/Pelodictyon group; Pelodictyon.
OX   NCBI_TaxID=324925 {ECO:0000313|EMBL:ACF44864.1, ECO:0000313|Proteomes:UP000002724};
RN   [1] {ECO:0000313|EMBL:ACF44864.1, ECO:0000313|Proteomes:UP000002724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5477 / BU-1 {ECO:0000313|Proteomes:UP000002724};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F., Overmann J.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of Pelodictyon phaeoclathratiforme BU-1.";
RL   Submitted (JUN-2008) 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=L-homoserine + ATP = O-phospho-L-homoserine + ADP + H(+);
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:ARBA00049375,
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}.
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DR   EMBL; CP001110; ACF44864.1; -; Genomic_DNA.
DR   RefSeq; WP_012509336.1; NC_011060.1.
DR   AlphaFoldDB; B4SGC8; -.
DR   STRING; 324925.Ppha_2706; -.
DR   KEGG; pph:Ppha_2706; -.
DR   eggNOG; COG0083; Bacteria.
DR   HOGENOM; CLU_041243_1_1_10; -.
DR   OrthoDB; 9769912at2; -.
DR   UniPathway; UPA00050; UER00064.
DR   Proteomes; UP000002724; 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:0009088; P:L-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; NF002288; PRK01212.1-4; 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000002724};
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..158
FT                   /note="GHMP kinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00288"
FT   DOMAIN          222..296
FT                   /note="GHMP kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08544"
FT   BINDING         100..110
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00384"
SQ   SEQUENCE   320 AA;  33679 MW;  BA334FFA511256AE CRC64;
     MKTVKGFASA TVGNVACGFD VLGFAITEPG DEVILTLSDR AHTDSPVSIS AITGDGGALP
     LDPKKNTSSF VVLKFLEYIR AHKQIDFTGH ISLELRKHLP LSSGMGSSAA SAAAALIAAN
     ELMGLPCSKM ELVHFAIEGE RVACGSAHAD NAAPAILGNF VLIRSYTPLD LITIPSPEHL
     YCSLVHPHTE LRTAYARSVL PQEISLKTAT QQWGNVGALV TGLLTSDYDL IGRSLVDVIA
     EPKRAPLIPG FFEVKQAALD SGALGCSIAG SGPSIFAFSS SEKTALAVGN AMKEAFLHSK
     AHLQSDMWVS PICKEGARIL
//