ID KHSE_SALG2 Reviewed; 309 AA.
AC B5REZ9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 01-MAY-2013, entry version 40.
DE RecName: Full=Homoserine kinase;
DE Short=HK;
DE Short=HSK;
DE EC=2.7.1.39;
GN Name=thrB; OrderedLocusNames=SG0003;
OS Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=550538;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=287/91 / NCTC 13346;
RX PubMed=18583645; DOI=10.1101/gr.077404.108;
RA Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K.,
RA Moule S., Mungall K., Saunders M., Whitehead S., Chabalgoity J.A.,
RA Maskell D., Humphreys T., Roberts M., Barrow P.A., Dougan G.,
RA Parkhill J.;
RT "Comparative genome analysis of Salmonella enteritidis PT4 and
RT Salmonella gallinarum 287/91 provides insights into evolutionary and
RT host adaptation pathways.";
RL Genome Res. 18:1624-1637(2008).
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of L-
CC homoserine to L-homoserine phosphate (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + L-homoserine = ADP + O-phospho-L-
CC homoserine.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
CC threonine from L-aspartate: step 4/5.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC -!- SIMILARITY: Belongs to the GHMP kinase family. Homoserine kinase
CC subfamily.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AM933173; CAR35913.1; -; Genomic_DNA.
DR RefSeq; YP_002225150.1; NC_011274.1.
DR ProteinModelPortal; B5REZ9; -.
DR STRING; 550538.SG0003; -.
DR PRIDE; B5REZ9; -.
DR EnsemblBacteria; CAR35913; CAR35913; SG0003.
DR GeneID; 6925030; -.
DR KEGG; seg:SG0003; -.
DR PATRIC; 18498077; VBISalEnt1629_0002.
DR eggNOG; COG0083; -.
DR HOGENOM; HOG000269560; -.
DR KO; K00872; -.
DR OMA; GFVHICK; -.
DR ProtClustDB; PRK01212; -.
DR BioCyc; SENT550538:GJ93-3-MONOMER; -.
DR UniPathway; UPA00050; UER00064.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0004413; F:homoserine kinase activity; IEA:HAMAP.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:HAMAP.
DR Gene3D; 3.30.230.10; -; 1.
DR HAMAP; MF_00384; Homoser_kinase; 1; -.
DR InterPro; IPR013750; GHMP_kinase_C_dom.
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 PRINTS; PR00958; HOMSERKINASE.
DR SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 1.
DR TIGRFAMs; TIGR00191; thrB; 1.
DR PROSITE; PS00627; GHMP_KINASES_ATP; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm;
KW Kinase; Nucleotide-binding; Threonine biosynthesis; Transferase.
FT CHAIN 1 309 Homoserine kinase.
FT /FTId=PRO_1000122439.
FT NP_BIND 91 101 ATP (Potential).
SQ SEQUENCE 309 AA; 33286 MW; 2B5D570CB35F8911 CRC64;
MVKVYAPASS ANMSVGFDVL GAAVTPVDGT LLGDVVSVEA ADHFRLHNLG RFADKLPPEP
RENIVYQCWE RFCQALGKTI PVAMTLEKNM PIGSGLGSSA CSVVAALVAM NEHCGKPLND
TRLLALMGEL EGRISGSIHY DNVAPCFLGG MQLMIEENGI ISQQVPGFDE WLWVLAYPGI
KVSTAEARAI LPAQYRRQDC IAHGRHLAGF IHACYSRQPQ LAAALMKDVI AEPYRARLLP
GFSQARQAVS EIGALASGIS GSGPTLFALC DKPETAQRVA DWLSKHYLQN QEGFVHICRL
DTAGARVVG
//
