ID F6EY31_SPHCR Unreviewed; 325 AA.
AC F6EY31;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
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=Sphch_1448 {ECO:0000313|EMBL:AEG49137.1};
OS Sphingobium chlorophenolicum L-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=690566 {ECO:0000313|EMBL:AEG49137.1, ECO:0000313|Proteomes:UP000007150};
RN [1] {ECO:0000313|EMBL:AEG49137.1, ECO:0000313|Proteomes:UP000007150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-1 {ECO:0000313|EMBL:AEG49137.1,
RC ECO:0000313|Proteomes:UP000007150};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Daligault H., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Pagani I., Turner P., Copley S., Woyke T.;
RT "Complete sequence of chromosome 1 of Sphingobium chlorophenolicum L-1.";
RL Submitted (MAY-2011) 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; CP002798; AEG49137.1; -; Genomic_DNA.
DR RefSeq; WP_013847398.1; NC_015593.1.
DR AlphaFoldDB; F6EY31; -.
DR STRING; 690566.Sphch_1448; -.
DR KEGG; sch:Sphch_1448; -.
DR HOGENOM; CLU_053300_1_0_5; -.
DR UniPathway; UPA00050; UER00064.
DR Proteomes; UP000007150; 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 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 Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697, ECO:0000256|HAMAP-
KW Rule:MF_00301};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00301, ECO:0000313|EMBL:AEG49137.1}.
FT DOMAIN 27..262
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
SQ SEQUENCE 325 AA; 35498 MW; 99C214EC0CEFE8F7 CRC64;
MAVYTQVSAE EIDAFLTRYD AGRLVSAKGI AEGVENSNYM LETTGHDGKG HRYILTLYEK
RVDEADLPFF MDLLDHLGAR GCLVPRFIAD RDGRRLQQLA GRPACLIEFL TGISVTEPTV
GQARAAGAAL GEMHRAAEGF TGTRRNALDL PGWHELAAKC GEDFDRIAPG LGARVAEELT
FLDAHWPSGL PRSVIHADLF PDNVLMLGDS VTGLIDFYFS CTDIRAYDLA VTHSAWCFSS
DGATWFAERA AALGAGYAAT HGLFEAERAA FPILCRGAAL RFLLTRAYDW INTPADALVT
RKDPLAYLRR LDFYASADPA MLLSA
//
