ID J9A4S6_9PROT Unreviewed; 328 AA.
AC J9A4S6;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=IMCC14465_11810 {ECO:0000313|EMBL:EJW21385.1};
OS alpha proteobacterium IMCC14465.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; PS1 clade.
OX NCBI_TaxID=1220535 {ECO:0000313|EMBL:EJW21385.1, ECO:0000313|Proteomes:UP000004836};
RN [1] {ECO:0000313|EMBL:EJW21385.1, ECO:0000313|Proteomes:UP000004836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC14465 {ECO:0000313|EMBL:EJW21385.1,
RC ECO:0000313|Proteomes:UP000004836};
RX PubMed=23209213; DOI=10.1128/JB.01888-12;
RA Yang S.J., Kang I., Cho J.C.;
RT "Genome Sequence of Strain IMCC14465, Isolated from the East Sea, Belonging
RT to the PS1 Clade of Alphaproteobacteria.";
RL J. Bacteriol. 194:6952-6953(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJW21385.1}.
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DR EMBL; ALYF01000003; EJW21385.1; -; Genomic_DNA.
DR AlphaFoldDB; J9A4S6; -.
DR STRING; 1220535.IMCC14465_11810; -.
DR PATRIC; fig|1220535.3.peg.1175; -.
DR eggNOG; COG2334; Bacteria.
DR OrthoDB; 9777460at2; -.
DR UniPathway; UPA00050; UER00064.
DR Proteomes; UP000004836; Unassembled WGS sequence.
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|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00301};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00301};
KW Reference proteome {ECO:0000313|Proteomes:UP000004836};
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:EJW21385.1}.
FT DOMAIN 27..263
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
SQ SEQUENCE 328 AA; 36444 MW; 481635E35C92EC6D CRC64;
MAVYTDLTDE QLTDLMSNYD IGNVLSLKGI AEGVENSNFL LTTDYNGQPK KFILTLYEKR
VNPDDLPFFI NLMTHLAESG LLCPVPVKRK DGATLSNIAG RPAAIISFLE GLSLRRPEAV
HCRALGASMA EMHLAAQRFD MTRANNLSID AWPALYETSR QNADTLHAGL TNLIDGELAR
LKELWPDAHA ALPRGIIHAD LFADNVFFIG TELSGIIDFY FACTDMLAYD LAIVLNAWCF
ETDTSFNITK ARALMDGYHS VRKLTPAEID ALPVLAAGAA MRFLLTRLHD WFAPQEGALV
KPKNPLDYLH RLRFHKKTKS AADYGVEI
//
