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Database: UniProt/TrEMBL
Entry: F6B967_DESCC
LinkDB: F6B967_DESCC
Original site: F6B967_DESCC 
ID   F6B967_DESCC            Unreviewed;       305 AA.
AC   F6B967;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   11-JUN-2014, entry version 18.
DE   RecName: Full=Homoserine kinase;
DE            Short=HK;
DE            Short=HSK;
DE            EC=2.7.1.39;
GN   Name=thrB; OrderedLocusNames=Desca_2000;
OS   Desulfotomaculum carboxydivorans (strain DSM 14880 / VKM B-2319 /
OS   CO-1-SRB).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfotomaculum.
OX   NCBI_TaxID=868595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14880 / VKM B-2319 / CO-1-SRB;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Lu M., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Stams A., Plugge C., Muyzer G.,
RA   Kuever J., Parshina S., Ivanova A., Nazina T., Woyke T.;
RT   "Complete sequence of Desulfotomaculum carboxydivorans CO-1-SRB.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. Homoserine kinase
CC       subfamily.
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DR   EMBL; CP002736; AEF94839.1; -; Genomic_DNA.
DR   RefSeq; YP_004497751.1; NC_015565.1.
DR   EnsemblBacteria; AEF94839; AEF94839; Desca_2000.
DR   GeneID; 10631418; -.
DR   KEGG; dca:Desca_2000; -.
DR   KO; K00872; -.
DR   BioCyc; DCAR868595:GHXC-2075-MONOMER; -.
DR   UniPathway; UPA00050; UER00064.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004413; F:homoserine kinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-HAMAP.
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; 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; Complete proteome; Cytoplasm;
KW   Kinase; Nucleotide-binding; Threonine biosynthesis; Transferase.
FT   NP_BIND      91    101       ATP (By similarity){EA2}.
SQ   SEQUENCE   305 AA;  32277 MW;  4F3D56A20C16ACD1 CRC64;
     MGMHKTVRVA VPATTANMGP GFDCLGMALN LYNEIYMSIS GDKLSIEVEG EGAMDISRDE
     QNIVYRAARR VYAELGQPVP GLTIKLVNKI PTSRGLGSSA AAIVGGLTAA NRLTGERLSQ
     ERLLELATEL EGHPDNVAPA LLGGIVISVL QDSKVHYLRI DPPAGLNTVV AIPDFPLSTR
     AAREVLPQRV SLQEAVFNLS RAALLVGALC EKRLDLLQVA GQDVLHQPHR ANLVPGMKEV
     MAAARQAGAL NVTLSGAGPT VIALTCGAEE AVAASMQHSF KQAGVNCHTK VLIPTIDGAQ
     IIWFN
//
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