KHSE_LACGA
ID KHSE_LACGA Reviewed; 287 AA.
AC Q043C5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=LGAS_1074;
OS Lactobacillus gasseri (strain ATCC 33323 / DSM 20243 / BCRC 14619 / CIP
OS 102991 / JCM 1131 / KCTC 3163 / NCIMB 11718 / NCTC 13722 / AM63).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=324831;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33323 / DSM 20243 / BCRC 14619 / CIP 102991 / JCM 1131 / KCTC
RC 3163 / NCIMB 11718 / NCTC 13722 / AM63;
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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; CP000413; ABJ60447.1; -; Genomic_DNA.
DR RefSeq; WP_003651647.1; NZ_WBMG01000002.1.
DR AlphaFoldDB; Q043C5; -.
DR SMR; Q043C5; -.
DR GeneID; 66469091; -.
DR KEGG; lga:LGAS_1074; -.
DR HOGENOM; CLU_041243_0_0_9; -.
DR OMA; CANRIPH; -.
DR OrthoDB; 610857at2; -.
DR BioCyc; LGAS324831:G1G6Y-1074-MON; -.
DR UniPathway; UPA00050; UER00064.
DR Proteomes; UP000000664; 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; -; 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..287
FT /note="Homoserine kinase"
FT /id="PRO_1000080124"
FT BINDING 78..88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00384"
SQ SEQUENCE 287 AA; 31498 MW; 3F33E53F89EA324F CRC64;
MKIFVPATSA NMGPGFDCLG TAVSMFLELD VLETSDKWFV EHDMSGISHD ESNLIVKTAL
ELAPKLTPHR LSVKSQIPLS RGLGSSSTAI VAGIELANQL ANLNLSQQDK CKIAAKIEGH
PDNVMPAILG GMVVASKIED QYYFQELPLI PFDFLAYIPN YELDTKASRN ALPEKLPFKN
ATHASSILGT LTASLALQDY GTAKRLIEAD EFHEPYRQKL VPELVKIRKI AHQHEAFATY
LSGAGSTVMT TIEHSRTEEF IASLRKAGLD DRIEQLKASS QGVFIEK
