(data stored in ACNUC7421 zone)

SWISSPROT: D1CDN4_THET1

ID   D1CDN4_THET1            Unreviewed;       303 AA.
AC   D1CDN4;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   08-MAY-2019, entry version 66.
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=Tter_0118 {ECO:0000313|EMBL:ACZ41040.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ41040.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ41040.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA   Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT   (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
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   -!- SIMILARITY: Belongs to the GHMP kinase family. Homoserine kinase
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00384,
CC       ECO:0000256|SAAS:SAAS00589914}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00384}.
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DR   EMBL; CP001825; ACZ41040.1; -; Genomic_DNA.
DR   STRING; 525904.Tter_0118; -.
DR   EnsemblBacteria; ACZ41040; ACZ41040; Tter_0118.
DR   KEGG; ttr:Tter_0118; -.
DR   eggNOG; ENOG4105D5I; Bacteria.
DR   eggNOG; COG0083; LUCA.
DR   HOGENOM; HOG000247199; -.
DR   KO; K00872; -.
DR   OMA; PDNVAPC; -.
DR   BioCyc; TTER525904:G1GGS-120-MONOMER; -.
DR   UniPathway; UPA00050; UER00064.
DR   Proteomes; UP000000323; Chromosome 1.
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; 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.
PE   3: Inferred from homology;
DR   PRODOM; D1CDN4.
DR   SWISS-2DPAGE; D1CDN4.
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:SAAS00483832};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00384};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00384,
KW   ECO:0000256|SAAS:SAAS00483829, ECO:0000313|EMBL:ACZ41040.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00384,
KW   ECO:0000256|SAAS:SAAS00483800};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323};
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:SAAS00129842}.
FT   DOMAIN       79    138       GHMP_kinases_N. {ECO:0000259|Pfam:
FT                                PF00288}.
FT   DOMAIN      217    267       GHMP_kinases_C. {ECO:0000259|Pfam:
FT                                PF08544}.
SQ   SEQUENCE   303 AA;  32264 MW;  EE9952B64876AA78 CRC64;
     MRIHVRVPAA SGNLGSGFDC AGMALALYNE AILDTDAKGV VIEGEGADFL PREESNACLK
     AMMELASRLD CQLPSFGLRL INRIPIGRGL ASSGAAALAG LLLANELLGC PKDREQIMEL
     ATELEGHPDN VAAALLGGIT ISAWDGSKVH TVRIDPDPSM KAVLWVPDSQ VYTKHARSIL
     PKQVSMQDAV FNLSRAALMA ASFARGEYNL LQVATQDRLH QPYRASLVKG LQESMLSALE
     AGALATWISG AGPSVLALCI DNVQAVELAL WHIASKYNDG KVMTLEIDTC GAQVTKMAEE
     VEV
//

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