ID A0A127JX33_9BURK Unreviewed; 326 AA.
AC A0A127JX33;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Homoserine kinase {ECO:0000256|HAMAP-Rule:MF_00301};
DE Short=HK {ECO:0000256|HAMAP-Rule:MF_00301};
DE Short=HSK {ECO:0000256|HAMAP-Rule:MF_00301};
DE EC=2.7.1.39 {ECO:0000256|HAMAP-Rule:MF_00301};
GN Name=thrB {ECO:0000256|HAMAP-Rule:MF_00301};
GN ORFNames=UC35_18315 {ECO:0000313|EMBL:AMO24433.1};
OS Ramlibacter tataouinensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ramlibacter.
OX NCBI_TaxID=94132 {ECO:0000313|EMBL:AMO24433.1, ECO:0000313|Proteomes:UP000070433};
RN [1] {ECO:0000313|EMBL:AMO24433.1, ECO:0000313|Proteomes:UP000070433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5-10 {ECO:0000313|EMBL:AMO24433.1,
RC ECO:0000313|Proteomes:UP000070433};
RX PubMed=24425747; DOI=10.1099/ijs.0.058396-0;
RA Lee H.J., Lee S.H., Lee S.S., Lee J.S., Kim Y., Kim S.C., Jeon C.O.;
RT "Ramlibacter solisilvae sp. nov., isolated from forest soil, and emended
RT description of the genus Ramlibacter.";
RL Int. J. Syst. Evol. Microbiol. 64:1317-1322(2014).
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_00301};
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 4/5. {ECO:0000256|HAMAP-Rule:MF_00301}.
CC -!- SIMILARITY: Belongs to the pseudomonas-type ThrB family.
CC {ECO:0000256|HAMAP-Rule:MF_00301}.
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DR EMBL; CP010951; AMO24433.1; -; Genomic_DNA.
DR RefSeq; WP_061502217.1; NZ_CP010951.1.
DR AlphaFoldDB; A0A127JX33; -.
DR PATRIC; fig|94132.3.peg.3743; -.
DR OrthoDB; 9777460at2; -.
DR UniPathway; UPA00050; UER00064.
DR Proteomes; UP000070433; Chromosome.
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 Gene3D; 3.90.1200.10; -; 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 NCBIfam; TIGR00938; thrB_alt; 1.
DR PANTHER; PTHR21064:SF6; APH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR21064; UNCHARACTERIZED; 1.
DR Pfam; PF01636; APH; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00301}; ATP-binding {ECO:0000256|HAMAP-Rule:MF_00301};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00301, ECO:0000313|EMBL:AMO24433.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00301};
KW Reference proteome {ECO:0000313|Proteomes:UP000070433};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697, ECO:0000256|HAMAP-
KW Rule:MF_00301};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00301, ECO:0000313|EMBL:AMO24433.1}.
FT DOMAIN 27..270
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
SQ SEQUENCE 326 AA; 36886 MW; FB15ADF90674A0B5 CRC64;
MAVFTEVSQE EAGELARKLG LGELRELRGI QGGIENTNYF LTTEQDGETL EYVLTLFERL
TFEQLPFYLH LMKHLALHRI PVPDPHELPG SETKEHPEGR LLHTVCGKPA AVVDRLRGKS
ELQPTAAHCD HVGDMLARMH LAARDYPRNQ PNLRGLAWWN ETVPVVLPYM DPAQAALLNA
ELAFQNHIAA GSAYAALPRG PIHADLFRDN VMFENGRLTG FFDFYFAGVD SWLFDIAVCL
NDWCIDLASG APDEEREQAF LAAYARVRPL AAAERQLLPA MLRAGALRFW VSRLWDFHLP
REAAMLKPHD PTHFERVLRQ RVAHAR
//
