(data stored in ACNUC7421 zone)

SWISSPROT: KHSE_ECODH

ID   KHSE_ECODH              Reviewed;         310 AA.
AC   B1XBC8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   05-JUL-2017, entry version 64.
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};
GN   OrderedLocusNames=ECDH10B_0003;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
CC   -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of L-
CC       homoserine to L-homoserine phosphate. {ECO:0000255|HAMAP-
CC       Rule:MF_00384}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-homoserine = ADP + O-phospho-L-
CC       homoserine. {ECO:0000255|HAMAP-Rule:MF_00384}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
CC       threonine from L-aspartate: step 4/5. {ECO:0000255|HAMAP-
CC       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}.
DR   EMBL; CP000948; ACB01208.1; -; Genomic_DNA.
DR   RefSeq; WP_000241662.1; NC_010473.1.
DR   ProteinModelPortal; B1XBC8; -.
DR   SMR; B1XBC8; -.
DR   EnsemblBacteria; ACB01208; ACB01208; ECDH10B_0003.
DR   KEGG; ecd:ECDH10B_0003; -.
DR   eggNOG; ENOG4105D5I; Bacteria.
DR   eggNOG; COG0083; LUCA.
DR   HOGENOM; HOG000247198; -.
DR   KO; K00872; -.
DR   OMA; PDNVAPC; -.
DR   UniPathway; UPA00050; UER00064.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004413; F:homoserine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
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;
DR   PRODOM; B1XBC8.
DR   SWISS-2DPAGE; B1XBC8.
KW   Amino-acid biosynthesis; ATP-binding; Cytoplasm; Kinase;
KW   Nucleotide-binding; Threonine biosynthesis; Transferase.
FT   CHAIN         1    310       Homoserine kinase.
FT                                /FTId=PRO_1000122420.
FT   NP_BIND      91    101       ATP. {ECO:0000255|HAMAP-Rule:MF_00384}.
SQ   SEQUENCE   310 AA;  33624 MW;  0F225F9F1B634BE8 CRC64;
     MVKVYAPASS ANMSVGFDVL GAAVTPVDGA LLGDVVTVEA AETFSLNNLG RFADKLPSEP
     RENIVYQCWE RFCQELGKQI PVAMTLEKNM PIGSGLGSSA CSVVAALMAM NEHCGKPLND
     TRLLALMGEL EGRISGSIHY DNVAPCFLGG MQLMIEENDI ISQQVPGFDE WLWVLAYPGI
     KVSTAEARAI LPAQYRRQDC IAHGRHLAGF IHACYSRQPE LAAKLMKDVI AEPYRERLLP
     GFRQARQAVA EIGAVASGIS GSGPTLFALC DKPETAQRVA DWLGKNYLQN QEGFVHICRL
     DTAGARVLEN
//

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