KHSE_BRADU
ID KHSE_BRADU Reviewed; 327 AA.
AC Q89UU4;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Homoserine kinase {ECO:0000255|HAMAP-Rule:MF_00301};
DE Short=HK {ECO:0000255|HAMAP-Rule:MF_00301};
DE Short=HSK {ECO:0000255|HAMAP-Rule:MF_00301};
DE EC=2.7.1.39 {ECO:0000255|HAMAP-Rule:MF_00301};
GN Name=thrB {ECO:0000255|HAMAP-Rule:MF_00301}; OrderedLocusNames=blr1315;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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:0000255|HAMAP-Rule:MF_00301};
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00301}.
CC -!- SIMILARITY: Belongs to the pseudomonas-type ThrB family.
CC {ECO:0000255|HAMAP-Rule:MF_00301}.
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DR EMBL; BA000040; BAC46580.1; -; Genomic_DNA.
DR RefSeq; NP_767955.1; NC_004463.1.
DR RefSeq; WP_011084133.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89UU4; -.
DR SMR; Q89UU4; -.
DR STRING; 224911.27349566; -.
DR EnsemblBacteria; BAC46580; BAC46580; BAC46580.
DR GeneID; 64021183; -.
DR KEGG; bja:blr1315; -.
DR PATRIC; fig|224911.44.peg.730; -.
DR eggNOG; COG2334; Bacteria.
DR HOGENOM; CLU_053300_1_0_5; -.
DR InParanoid; Q89UU4; -.
DR OMA; DPTHFER; -.
DR PhylomeDB; Q89UU4; -.
DR UniPathway; UPA00050; UER00064.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0019202; F:amino acid kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004413; F:homoserine kinase activity; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009088; P:threonine biosynthetic process; IBA:GO_Central.
DR CDD; cd05153; HomoserineK_II; 1.
DR HAMAP; MF_00301; Homoser_kinase_2; 1.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR005280; Homoserine_kinase_II.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR Pfam; PF01636; APH; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR TIGRFAMs; TIGR00938; thrB_alt; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; ATP-binding; Kinase; Nucleotide-binding;
KW Reference proteome; Threonine biosynthesis; Transferase.
FT CHAIN 1..327
FT /note="Homoserine kinase"
FT /id="PRO_0000172185"
SQ SEQUENCE 327 AA; 35819 MW; E141F9F97F66CF79 CRC64;
MAVYTDVAAD ELADFLSQYD LGELLSYKGI AEGVENSNFL LHTTKGSFIL TLYEKRVAKN
DLPFFLALMT HLAEHGVNCP LPVKGRDGEA LRELSGRPAA IITFLEGVWP RKPNAAHCAG
VGEGLARMHL AGANFAIRRA NALSVAGWRP LFDAAASRAD EVQPGLRAFL AAELDYLASG
VWPTNLPEGV IHADLFNDNV FFLGDKLSGI IDFTFACNDM LAYDVAICLN AWCFEPDHSF
NVTKARAFLN AYGRVRKLSE AEEAALPLLA RGAAIRFLLT RLVDWLNVPP GALVRPKDPL
EYVRKLRFHQ SVSSVRDYGL MPSGLVA
