KHSE_CHESB
ID KHSE_CHESB Reviewed; 322 AA.
AC Q11KC6;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=Meso_0749;
OS Chelativorans sp. (strain BNC1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Chelativorans; unclassified Chelativorans.
OX NCBI_TaxID=266779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BNC1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of chromosome of Mesorhizobium sp. BNC1.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000390; ABG62149.1; -; Genomic_DNA.
DR RefSeq; WP_011580092.1; NC_008254.1.
DR AlphaFoldDB; Q11KC6; -.
DR SMR; Q11KC6; -.
DR STRING; 266779.Meso_0749; -.
DR PRIDE; Q11KC6; -.
DR EnsemblBacteria; ABG62149; ABG62149; Meso_0749.
DR KEGG; mes:Meso_0749; -.
DR eggNOG; COG2334; Bacteria.
DR HOGENOM; CLU_053300_0_0_5; -.
DR OMA; DPTHFER; -.
DR OrthoDB; 1003984at2; -.
DR UniPathway; UPA00050; UER00064.
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..322
FT /note="Homoserine kinase"
FT /id="PRO_0000300794"
SQ SEQUENCE 322 AA; 36289 MW; BB2B9EE2742386BB CRC64;
MAVYTDISEE ELTAFLRHYP VGKLLSYKGI AEGTENSNYL LHTTAGAYIL TLYERRVDRS
DLPFFLGLME HLARKGVSCP LPVKRLDDGL IGELAGRPAA LITFLEGMWM RRPTALHCGQ
VGKALADLHQ AAEDFPLKRP NALGPEGWRR LWEGAKARAD EVEPGLAREV DAEFALLERD
WPKDLPSGVI HADLFPDNVF FLGGELSGLI DFYFACNDLL AYDLATCLNA WCFEKDISYN
LTKGAALLAG YQAVRPLTRE EIEMLPLLAR GSALRFMLTR LYDWLTIPDG ALVKKRDPLE
YLRRLRFHRQ VRTASEYGIE LA