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KHSE_ALIF1
ID   KHSE_ALIF1              Reviewed;         318 AA.
AC   Q5E2Y4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=VF_2117;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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; CP000020; AAW86612.1; -; Genomic_DNA.
DR   RefSeq; WP_005420768.1; NC_006840.2.
DR   RefSeq; YP_205500.1; NC_006840.2.
DR   AlphaFoldDB; Q5E2Y4; -.
DR   SMR; Q5E2Y4; -.
DR   STRING; 312309.VF_2117; -.
DR   EnsemblBacteria; AAW86612; AAW86612; VF_2117.
DR   GeneID; 64242751; -.
DR   KEGG; vfi:VF_2117; -.
DR   PATRIC; fig|312309.11.peg.2160; -.
DR   eggNOG; COG0083; Bacteria.
DR   HOGENOM; CLU_041243_1_1_6; -.
DR   OMA; CANRIPH; -.
DR   OrthoDB; 610857at2; -.
DR   UniPathway; UPA00050; UER00064.
DR   Proteomes; UP000000537; Chromosome I.
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; Reference proteome; Threonine biosynthesis;
KW   Transferase.
FT   CHAIN           1..318
FT                   /note="Homoserine kinase"
FT                   /id="PRO_1000049195"
FT   BINDING         97..107
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00384"
SQ   SEQUENCE   318 AA;  34580 MW;  AC10B6E66A0F4443 CRC64;
     MSVVVYAPAS IGNVSVGFDV LGAAVSPIDG TLLGDRVLVE LGSEAFTLAT AGSFVDKLPE
     NPKDNIVYDC WCVFSRELNK KNVALKNVHM ILEKNMPIGS GLGSSACSIV AALDALNQFH
     DNPLNDMELL ALMGEMEGQI SGGIHYDNVA PCYLGGLQLM VEELGIISQE VPCFDEWYWV
     MAYPGIKVST AEAREILPSQ YRRQDVIAHG RNLAGFIHAC YSKQPELAAK MIKDVVAEPY
     RERLLPNFAK AREYAASAGA LTTGISGSGP TLFSICKDKD VADRVSRWLQ ENYVQNNEGF
     VHVCRLDKQG SQVTGSKL
 
 
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