KHSE_LISMO
ID KHSE_LISMO Reviewed; 288 AA.
AC Q8Y4A6;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=lmo2545;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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; AL591983; CAD00623.1; -; Genomic_DNA.
DR PIR; AI1392; AI1392.
DR RefSeq; NP_466068.1; NC_003210.1.
DR RefSeq; WP_010990012.1; NZ_CP023861.1.
DR PDB; 3HUL; X-ray; 2.19 A; A/B=2-288.
DR PDBsum; 3HUL; -.
DR AlphaFoldDB; Q8Y4A6; -.
DR SMR; Q8Y4A6; -.
DR STRING; 169963.lmo2545; -.
DR PaxDb; Q8Y4A6; -.
DR DNASU; 984754; -.
DR EnsemblBacteria; CAD00623; CAD00623; CAD00623.
DR GeneID; 984754; -.
DR KEGG; lmo:lmo2545; -.
DR PATRIC; fig|169963.11.peg.2607; -.
DR eggNOG; COG0083; Bacteria.
DR HOGENOM; CLU_041243_0_0_9; -.
DR OMA; CANRIPH; -.
DR PhylomeDB; Q8Y4A6; -.
DR BioCyc; LMON169963:LMO2545-MON; -.
DR UniPathway; UPA00050; UER00064.
DR EvolutionaryTrace; Q8Y4A6; -.
DR Proteomes; UP000000817; 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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; ATP-binding; Cytoplasm; Kinase;
KW Nucleotide-binding; Reference proteome; Threonine biosynthesis;
KW Transferase.
FT CHAIN 1..288
FT /note="Homoserine kinase"
FT /id="PRO_0000156584"
FT BINDING 79..89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00384"
FT STRAND 2..11
FT /evidence="ECO:0007829|PDB:3HUL"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:3HUL"
FT STRAND 19..34
FT /evidence="ECO:0007829|PDB:3HUL"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:3HUL"
FT HELIX 55..63
FT /evidence="ECO:0007829|PDB:3HUL"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:3HUL"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:3HUL"
FT HELIX 86..101
FT /evidence="ECO:0007829|PDB:3HUL"
FT HELIX 108..119
FT /evidence="ECO:0007829|PDB:3HUL"
FT HELIX 125..130
FT /evidence="ECO:0007829|PDB:3HUL"
FT STRAND 132..139
FT /evidence="ECO:0007829|PDB:3HUL"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:3HUL"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:3HUL"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:3HUL"
FT HELIX 179..196
FT /evidence="ECO:0007829|PDB:3HUL"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:3HUL"
FT HELIX 201..208
FT /evidence="ECO:0007829|PDB:3HUL"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:3HUL"
FT HELIX 225..233
FT /evidence="ECO:0007829|PDB:3HUL"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:3HUL"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:3HUL"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:3HUL"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:3HUL"
FT HELIX 258..266
FT /evidence="ECO:0007829|PDB:3HUL"
FT STRAND 271..279
FT /evidence="ECO:0007829|PDB:3HUL"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:3HUL"
SQ SEQUENCE 288 AA; 30832 MW; ACBFF423466B7D23 CRC64;
MRIRVPATTA NLGPGFDSCG LALTLYLTLD IGAEADSWYI EHNIGGGIPH DETNVIIETA
LNLAPNLTPH HLVMTCDIPP ARGLGSSSAA VVAGIELANT LAELNLSKEE KVRIAAEIEG
HPDNVAPAVL GNWVVGAKLD GEDFYVRHLF PDCALIAFIP KAELLTSESR GVLPDTLPFK
EAVQASSIAN VMIAAILRND MTLAGEMMER DLWHEKYRSQ LVPHLAQIRD VAKNQGAYAA
CLSGAGPTVL VFAPRNLANK LQTSLQTLEI DADVLLLDVE GSGAEVFR
