ID A0A1I4QYC7_9PSED Unreviewed; 316 AA.
AC A0A1I4QYC7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=SAMN04487858_10340 {ECO:0000313|EMBL:SFM45082.1};
OS Pseudomonas sp. ok602.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1761898 {ECO:0000313|EMBL:SFM45082.1, ECO:0000313|Proteomes:UP000199362};
RN [1] {ECO:0000313|Proteomes:UP000199362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK602 {ECO:0000313|Proteomes:UP000199362};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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: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; FOUL01000003; SFM45082.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4QYC7; -.
DR STRING; 1761898.SAMN04487858_10340; -.
DR OrthoDB; 9777460at2; -.
DR UniPathway; UPA00050; UER00064.
DR Proteomes; UP000199362; 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|HAMAP-Rule:MF_00301, ECO:0000313|EMBL:SFM45082.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00301};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697, ECO:0000256|HAMAP-
KW Rule:MF_00301}; Transferase {ECO:0000256|HAMAP-Rule:MF_00301}.
FT DOMAIN 27..255
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
SQ SEQUENCE 316 AA; 34968 MW; 2442B4089C367398 CRC64;
MSVFTPLARP ELETFLAPYG LGRLLDFQGI AAGSENTNFF ISLERGECVL TLVERGPVQE
MPFFIELLDV LHDANLPVPY ALRTTDGVAL RTLAGKPALL QPRLAGKHIK VANAQHCVQV
GELLGHLHLA TKDQMIPRKT DRGLDWMLEQ GTQLLSHLAT EPRELLQRAL DEISAQKANI
LALPQANIHA DLFRDNAMFE GTHLTGLIDF YNACSGPMLY DVAIALNDWC ADDDGVIDGP
RARALLGAYA ALRPFTAAEA ELWPTLLRVA CVRFWLSRLI AAESFAGQDV LIHDPMEFQQ
RLTQRQQVST PLPFAL
//
