ID   A4ISF3_GEOTN            Unreviewed;       304 AA.
AC   A4ISF3;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 108.
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=GTNG_2912 {ECO:0000313|EMBL:ABO68257.1};
OS   Geobacillus thermodenitrificans (strain NG80-2).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=420246 {ECO:0000313|EMBL:ABO68257.1, ECO:0000313|Proteomes:UP000001578};
RN   [1] {ECO:0000313|EMBL:ABO68257.1, ECO:0000313|Proteomes:UP000001578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NG80-2 {ECO:0000313|EMBL:ABO68257.1,
RC   ECO:0000313|Proteomes:UP000001578};
RX   PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA   Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA   Han W., Peng X., Liu R., Wang L.;
RT   "Genome and proteome of long-chain alkane degrading Geobacillus
RT   thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
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}.
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DR   EMBL; CP000557; ABO68257.1; -; Genomic_DNA.
DR   RefSeq; WP_011888121.1; NC_009328.1.
DR   AlphaFoldDB; A4ISF3; -.
DR   KEGG; gtn:GTNG_2912; -.
DR   eggNOG; COG0083; Bacteria.
DR   HOGENOM; CLU_041243_0_0_9; -.
DR   UniPathway; UPA00050; UER00064.
DR   Proteomes; UP000001578; 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          83..143
FT                   /note="GHMP kinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00288"
FT   DOMAIN          204..280
FT                   /note="GHMP kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08544"
FT   BINDING         90..100
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00384"
SQ   SEQUENCE   304 AA;  32946 MW;  4E8079118E217B6D CRC64;
     MKEDEMLKIV VPGSTANLGP GFDSVGLAVS RYLTLDVRLA RTWSFTPKTA EVSDIPRGTD
     NLVYKVANET AKAHGRQLPS CEVDVYSDIP FTRGLGSSAA AVVAGIELAD ALLELGLTRE
     QKMELATRYE GHPDNVGASL YGGLVIGCYR EAGVDVVHVP ELAIELVAII PAYELETKKA
     RGQLPEQWMR QQAVEASAIS NVLVAALLTK NWKLAGRMMA ADLFHQPYRK SLVPELERAQ
     ALAEEYEAIG AALSGAGPTV LVFAEPGKGE QLERQLRPHF PACEVTWLAI EPHGSRVYKL
     ALEA
//