ID A0A1H9X1V2_9BACI Unreviewed; 306 AA.
AC A0A1H9X1V2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Homoserine kinase {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|HAMAP-Rule:MF_00384};
GN Name=thrB {ECO:0000256|HAMAP-Rule:MF_00384};
GN ORFNames=SAMN05518684_12317 {ECO:0000313|EMBL:SES40172.1};
OS Salipaludibacillus aurantiacus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae.
OX NCBI_TaxID=1601833 {ECO:0000313|EMBL:SES40172.1, ECO:0000313|Proteomes:UP000198571};
RN [1] {ECO:0000313|EMBL:SES40172.1, ECO:0000313|Proteomes:UP000198571}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S9 {ECO:0000313|EMBL:SES40172.1,
RC ECO:0000313|Proteomes:UP000198571};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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|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|HAMAP-Rule:MF_00384}.
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DR EMBL; FOGT01000023; SES40172.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9X1V2; -.
DR STRING; 1601833.SAMN05518684_12317; -.
DR OrthoDB; 9769912at2; -.
DR UniPathway; UPA00050; UER00064.
DR Proteomes; UP000198571; Unassembled WGS sequence.
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; 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.
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 81..142
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 203..280
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
FT BINDING 89..99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00384"
SQ SEQUENCE 306 AA; 33198 MW; F553087AF970FF2D CRC64;
MSNSPFTIRV PASTANLGPG FDSVGMALNR YLMLTVEPGD TWRFEAQSDN LEGIPAGKDN
LIFKIADWIA DEYGEDLPSA HVKMDSDIPL SRGFGSSATA IVAGIELANQ LLGLELPADE
KARWASQYEG HPDNVAPSVY GGLIIGSHRD EETDIVLAGT PDIDLVAVIP DYELSTKESR
DTLPKEFSYR DAVEASSISN VLVAAILQGN WELAGKMMTK DLFHLPFRMP HIPEWQKAAE
LTGELPVYGA TLSGAGPIVL FFVPRGYGKE VRLQLRGHFP SHSVELLEVD RDGVVVSAHA
VSSNQL
//
