KHSE_CUPTR
ID KHSE_CUPTR Reviewed; 334 AA.
AC B3R5F6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=RALTA_A2247;
OS Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS 107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=977880;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 / R1;
RX PubMed=18490699; DOI=10.1101/gr.076448.108;
RA Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA Masson-Boivin C.;
RT "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT comparative genomics of rhizobia.";
RL Genome Res. 18:1472-1483(2008).
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; CU633749; CAQ70181.1; -; Genomic_DNA.
DR RefSeq; WP_012353486.1; NC_010528.1.
DR AlphaFoldDB; B3R5F6; -.
DR SMR; B3R5F6; -.
DR STRING; 977880.RALTA_A2247; -.
DR EnsemblBacteria; CAQ70181; CAQ70181; RALTA_A2247.
DR GeneID; 29762606; -.
DR KEGG; cti:RALTA_A2247; -.
DR eggNOG; COG2334; Bacteria.
DR HOGENOM; CLU_053300_0_0_4; -.
DR OMA; DPTHFER; -.
DR OrthoDB; 1003984at2; -.
DR BioCyc; CTAI977880:RALTA_RS10895-MON; -.
DR UniPathway; UPA00050; UER00064.
DR Proteomes; UP000001692; Chromosome 1.
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..334
FT /note="Homoserine kinase"
FT /id="PRO_1000115431"
SQ SEQUENCE 334 AA; 38131 MW; 7557BD975A5945DC CRC64;
MAVFTTVSQD EIARWLLDFD LGEVRELRGI ASGIENSNFF LTMEHEGQTR QYVLTIFERL
SFTQLPYYLH LMAHLAERGI RVPAPIPARD GEILRPLKGK PATIVTRLPG ASQLAPDAQH
CAEVGDMLAR MHLAGADYPR RQPNLRSLPW WQQTEREILP FLDAGQRALL QREIAHQAAF
FASAAYASLG EGPCHCDLFR DNALFEEDAS GRHRLGGFFD FYFAGNDKWL FDVAVTVNDW
CIDLATGELD AERAQALLRA YHAVRPLTET EAAHWQDMLR AGALRFWVSR LWDFYLPREA
DMLQPHDPTH FERILRRRLD AQPANPESAP LPWI
