(data stored in ACNUC7421 zone)

SWISSPROT: KHSE_SULIK

ID   KHSE_SULIK              Reviewed;         311 AA.
AC   C4KK76;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 45.
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=M164_0183;
OS   Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=426118;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.4 / Kamchatka #3;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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; CP001402; ACR40817.1; -; Genomic_DNA.
DR   RefSeq; WP_012710342.1; NC_012726.1.
DR   ProteinModelPortal; C4KK76; -.
DR   SMR; C4KK76; -.
DR   EnsemblBacteria; ACR40817; ACR40817; M164_0183.
DR   GeneID; 7813857; -.
DR   KEGG; sid:M164_0183; -.
DR   HOGENOM; HOG000247197; -.
DR   KO; K00872; -.
DR   OMA; PDNVAPC; -.
DR   OrthoDB; POG093Z0AGJ; -.
DR   BioCyc; SISL426118:GI01-185-MONOMER; -.
DR   UniPathway; UPA00050; UER00064.
DR   Proteomes; UP000001479; Chromosome.
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   PANTHER; PTHR20861:SF8; PTHR20861:SF8; 1.
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; C4KK76.
DR   SWISS-2DPAGE; C4KK76.
KW   Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm;
KW   Kinase; Nucleotide-binding; Threonine biosynthesis; Transferase.
FT   CHAIN         1    311       Homoserine kinase.
FT                                /FTId=PRO_1000205742.
FT   NP_BIND      88     98       ATP. {ECO:0000255|HAMAP-Rule:MF_00384}.
SQ   SEQUENCE   311 AA;  33887 MW;  324E198A7D5AC43F CRC64;
     MECKRARAYS SSANLGSGFD ILSMAHTAFF DTVEICVETK NSENIVIESN SKIPLEPNRN
     SATYPLVRIM EERGIKASLR VKVIKGIPEG LGLGSSGASA TAAVMAFSSL FNLNLSKEDL
     VRYAMYGEIA SSGSPHPDNV AASVFGGVVS VVSVNPVKVV EIPLNYSFNI LLFVPLNVHI
     EEKTKKAREM VPKTVKLSDY INNSRYISSL LIGFVKGERD LIRLGLNDEI VEKARLPLFP
     YYPKIKEIAI KYDAVGSCVS GAGPSILVLT DKMTDENKIA EEGTKTCNEF NVECEVIKAK
     IAGGVEVERR N
//

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