KHSE_BURM9
ID KHSE_BURM9 Reviewed; 331 AA.
AC A2S0L3; A2S0L2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
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};
GN OrderedLocusNames=BMA10229_1681;
OS Burkholderia mallei (strain NCTC 10229).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=412022;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 10229;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(2010).
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; CP000545; ABN00147.2; -; Genomic_DNA.
DR RefSeq; WP_004190439.1; NC_008835.1.
DR AlphaFoldDB; A2S0L3; -.
DR SMR; A2S0L3; -.
DR EnsemblBacteria; ABN00147; ABN00147; BMA10229_1681.
DR GeneID; 56598211; -.
DR KEGG; bml:BMA10229_1681; -.
DR HOGENOM; CLU_053300_0_0_4; -.
DR OMA; DPTHFER; -.
DR UniPathway; UPA00050; UER00064.
DR Proteomes; UP000002283; Chromosome II.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004413; F:homoserine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniRule.
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 Threonine biosynthesis; Transferase.
FT CHAIN 1..331
FT /note="Homoserine kinase"
FT /id="PRO_1000022578"
SQ SEQUENCE 331 AA; 36779 MW; 587176329DF0897C CRC64;
MAVFTAVSDA DLALWMRHYD LGDVVAFRGI PSGIENSNFF LTTTRGEYVL TIFENLTAGQ
LPFYVDLMSH LAKHGVPVPA PVARDDGTLF GELHGKPAAI VTKLEGAAQL APGVEHCVEV
GQMLARMHLA GRDYPRHQPN LRSLPWWRDT VPAIAPFVTG EQRALLEGEL AHQAAFFASD
DYAALPEGPC HCDLFRDNAL FAHAEPDTGH SVRLGGFFDF YFAGCDKWLF DVAVTVNDWC
VDLPTGALDA ARADALLRAY QTVRPFTAGE RRRWGDMLRA GAYRFWVSRL YDFHLPRAAQ
MLKPHDPGHF ERILRERIAH AGALPETHAC N