KHSE_MYCSJ
ID KHSE_MYCSJ Reviewed; 314 AA.
AC A3Q3C9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Homoserine kinase {ECO:0000255|HAMAP-Rule:MF_00384};
DE Short=HK {ECO:0000255|HAMAP-Rule:MF_00384};
DE Short=HSK {ECO:0000255|HAMAP-Rule:MF_00384};
DE EC=2.7.1.39 {ECO:0000255|HAMAP-Rule:MF_00384};
GN Name=thrB {ECO:0000255|HAMAP-Rule:MF_00384}; OrderedLocusNames=Mjls_3880;
OS Mycobacterium sp. (strain JLS).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; unclassified Mycobacterium.
OX NCBI_TaxID=164757;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLS;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Anderson A.J.,
RA Sims R.C., Richardson P.;
RT "Complete sequence of Mycobacterium sp. JLS.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of L-homoserine
CC to L-homoserine phosphate. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00384};
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00384}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00384}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. Homoserine kinase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00384}.
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DR EMBL; CP000580; ABN99656.1; -; Genomic_DNA.
DR AlphaFoldDB; A3Q3C9; -.
DR SMR; A3Q3C9; -.
DR STRING; 164757.Mjls_3880; -.
DR KEGG; mjl:Mjls_3880; -.
DR HOGENOM; CLU_041243_0_1_11; -.
DR OMA; CANRIPH; -.
DR BioCyc; MSP164757:G1G8C-3920-MON; -.
DR UniPathway; UPA00050; UER00064.
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; -; 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_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR Pfam; PF08544; GHMP_kinases_C; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR PIRSF; PIRSF000676; Homoser_kin; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55060; SSF55060; 1.
DR TIGRFAMs; TIGR00191; thrB; 1.
DR PROSITE; PS00627; GHMP_KINASES_ATP; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; ATP-binding; Cytoplasm; Kinase;
KW Nucleotide-binding; Threonine biosynthesis; Transferase.
FT CHAIN 1..314
FT /note="Homoserine kinase"
FT /id="PRO_1000049148"
FT BINDING 95..105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00384"
SQ SEQUENCE 314 AA; 31860 MW; EE3CF88C309FC30B CRC64;
MTQTLPAGLT ATAMVAASSA NLGPGFDSLG LALSLYDEIV VETVDSGLTV TVEGEGAGQV
ALDSSHLVVR AIEAGLRATG CVAPGLVVRC RNDIPHSRGL GSSAAAVVGG LAAANGLVSQ
TDWTPLTVEQ LIQLSSAFEG HPDNAAAAVL GGAVVTWTDG AGAQARYAAA PLRVHPDIHL
FPAIPQQRSS TAETRVLLPD TVSHTDARFN LSRAALLVVA LTERPDLLMA ATEDVLHQPQ
RAAAMPASAE FLRVLRGCGV AAVLSGAGPA VIALSTEPEL PAEAVEFGIA NGFTIAEMAV
GDGVRWSTGV AAGR