(data stored in ACNUC7421 zone)

SWISSPROT: A0A0F6BIW2_GEOS0

ID   A0A0F6BIW2_GEOS0        Unreviewed;       304 AA.
AC   A0A0F6BIW2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, entry version 24.
DE   RecName: Full=Homoserine kinase {ECO:0000256|HAMAP-Rule:MF_00384, ECO:0000256|SAAS:SAAS01095763};
DE            Short=HK {ECO:0000256|HAMAP-Rule:MF_00384};
DE            Short=HSK {ECO:0000256|HAMAP-Rule:MF_00384};
DE            EC=2.7.1.39 {ECO:0000256|HAMAP-Rule:MF_00384, ECO:0000256|SAAS:SAAS00405466};
GN   Name=thrB {ECO:0000256|HAMAP-Rule:MF_00384};
GN   OrderedLocusNames=GY4MC1_0531 {ECO:0000313|EMBL:ADP73363.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73363.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73363.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73363.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of L-
CC       homoserine to L-homoserine phosphate. {ECO:0000256|HAMAP-
CC       Rule:MF_00384, ECO:0000256|SAAS:SAAS01095782}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-homoserine = ADP + H(+) + O-phospho-L-homoserine;
CC         Xref=Rhea:RHEA:13985, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57476, ChEBI:CHEBI:57590, ChEBI:CHEBI:456216;
CC         EC=2.7.1.39; Evidence={ECO:0000256|HAMAP-Rule:MF_00384,
CC         ECO:0000256|SAAS:SAAS01127705};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
CC       threonine from L-aspartate: step 4/5. {ECO:0000256|HAMAP-
CC       Rule:MF_00384, ECO:0000256|SAAS:SAAS00129811}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00384,
CC       ECO:0000256|SAAS:SAAS01090001}.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. Homoserine kinase
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00384,
CC       ECO:0000256|SAAS:SAAS00589914}.
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DR   EMBL; CP002293; ADP73363.1; -; Genomic_DNA.
DR   RefSeq; WP_013400076.1; NC_014650.1.
DR   EnsemblBacteria; ADP73363; ADP73363; GY4MC1_0531.
DR   GeneID; 29236814; -.
DR   KEGG; gmc:GY4MC1_0531; -.
DR   KO; K00872; -.
DR   OMA; PDNVAPC; -.
DR   OrthoDB; 610857at2; -.
DR   BioCyc; GSP581103:G1GOQ-582-MONOMER; -.
DR   UniPathway; UPA00050; UER00064.
DR   Proteomes; UP000002034; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004413; F:homoserine kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniRule.
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; IPR036554; GHMP_kinase_C_sf.
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; A0A0F6BIW2.
DR   SWISS-2DPAGE; A0A0F6BIW2.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00384,
KW   ECO:0000256|SAAS:SAAS00483757};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00384,
KW   ECO:0000256|SAAS:SAAS00456406};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00384,
KW   ECO:0000256|SAAS:SAAS01089967};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00384,
KW   ECO:0000256|SAAS:SAAS00456396, ECO:0000313|EMBL:ADP73363.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00384,
KW   ECO:0000256|SAAS:SAAS00456300};
KW   Threonine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00384,
KW   ECO:0000256|SAAS:SAAS00483747};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00384,
KW   ECO:0000256|SAAS:SAAS00456450}.
FT   DOMAIN       84    143       GHMP_kinases_N. {ECO:0000259|Pfam:
FT                                PF00288}.
FT   DOMAIN      204    275       GHMP_kinases_C. {ECO:0000259|Pfam:
FT                                PF08544}.
FT   NP_BIND      90    100       ATP. {ECO:0000256|HAMAP-Rule:MF_00384}.
SQ   SEQUENCE   304 AA;  32900 MW;  701688081EE72F63 CRC64;
     MKEDGMLRIV VPASTANLGP GFDSIGLAVS RYLTLEVRLA DEWKFVPRSS EVAAIPAGMD
     NLIYQVAAQV AQTYGCTLPS CFVDVYSNIP FTRGLGSSAA AVVAGIELAN ELAGLSLSLE
     QKMRFASCYE GHPDNVGASL YGGLVIGSHR REETDVVHVP DVQLDLVAVI PSYELETEKA
     RSVLPQMMAR EDAVEASAVS NVLVAALLTK RWELAGKMMS CDLFHQPYRK ELVPQLSLVE
     KLAMQYGAFG VALSGAGPTI LAFAEPGKGM ELKEKLAPYF PDCAVEWLTV EQKGSQVYKM
     SFEK
//

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