ID   KHSE_CHLTE              Reviewed;         324 AA.
AC   Q8KAW7;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 42.
DE   RecName: Full=Homoserine kinase;
DE            Short=HSK;
DE            Short=HK;
DE            EC=2.7.1.39;
GN   Name=thrB; OrderedLocusNames=CT2034;
OS   Chlorobium tepidum.
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobaculum.
OX   NCBI_TaxID=1097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / TLS;
RX   MEDLINE=22103685; PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M.,
RA   Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F.,
RA   Holt I.E., Umayam L.A., Mason T.M., Brenner M., Shea T.P.,
RA   Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B.,
RA   Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M.,
RA   Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a
RT   photosynthetic, anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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.
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DR   EMBL; AE006470; AAM73251.1; -; Genomic_DNA.
DR   RefSeq; NP_662909.1; -.
DR   HSSP; Q58504; 1H74.
DR   GeneID; 1007526; -.
DR   GenomeReviews; AE006470_GR; CT2034.
DR   KEGG; cte:CT2034; -.
DR   NMPDR; fig|194439.1.peg.2003; -.
DR   TIGR; CT2034; -.
DR   HOGENOM; Q8KAW7; -.
DR   OMA; Q8KAW7; CGSAHAD.
DR   BioCyc; CTEP194439:CT_2034-MON; -.
DR   BRENDA; 2.7.1.39; 189605.
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:0016310; P:phosphorylation; IEA:InterPro.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00384; -; 1.
DR   InterPro; IPR006204; GHMP_kinase.
DR   InterPro; IPR013750; GHMP_kinase_C.
DR   InterPro; IPR006203; GHMP_knse_ATP_bd_CS.
DR   InterPro; IPR000870; Homoserine_kin.
DR   InterPro; IPR014721; Ribosomal_S5_D2-type_fold.
DR   Gene3D; G3DSA:3.30.230.10; Ribosomal_S5_D2-type_fold; 1.
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   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    324       Homoserine kinase.
FT                                /FTId=PRO_0000156560.
FT   NP_BIND     100    110       ATP (Potential).
SQ   SEQUENCE   324 AA;  33771 MW;  DA228CBDC45330DE CRC64;
     MKTVTGFASA TVGNVACGFD VLGFAITEPG DEVVLALHDE RRSDCPVSIT SIVGDGGALP
     LDPKKNTSSF VVLKFLEYIR TTKGISFDGH IDLVLKKNLP LSSGMGSSAA SAAAALIAAN
     ELFGSPCTKM ELVHFAIEGE RVACGSAHAD NAAPAMLGNF ILIRSYNPLD LITIKPPKNL
     FGTLVHPHTE LKTSFARSVL PKSIPLSTAT QQWGNVGALI AGLLMEDYDL IGRALVDVVA
     EPKRAPLIPG FNEVKQAALD AGALGCSIAG SGPSVFAFSS SRQTAEAVGS AMQSAFLHSR
     AALQSDMWVS PICSQGARII STTS
//