KHSE_ACICJ
ID KHSE_ACICJ Reviewed; 319 AA.
AC A5FZ25;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=Acry_1652;
OS Acidiphilium cryptum (strain JF-5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=349163;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JF-5;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.;
RT "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL Submitted (MAY-2007) 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: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; CP000697; ABQ30857.1; -; Genomic_DNA.
DR RefSeq; WP_011942400.1; NC_009484.1.
DR AlphaFoldDB; A5FZ25; -.
DR SMR; A5FZ25; -.
DR STRING; 349163.Acry_1652; -.
DR EnsemblBacteria; ABQ30857; ABQ30857; Acry_1652.
DR KEGG; acr:Acry_1652; -.
DR eggNOG; COG2334; Bacteria.
DR HOGENOM; CLU_053300_1_0_5; -.
DR OMA; DPTHFER; -.
DR OrthoDB; 1003984at2; -.
DR UniPathway; UPA00050; UER00064.
DR Proteomes; UP000000245; 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 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 Reference proteome; Threonine biosynthesis; Transferase.
FT CHAIN 1..319
FT /note="Homoserine kinase"
FT /id="PRO_1000022574"
SQ SEQUENCE 319 AA; 34972 MW; 54A2F8B8A4B0F12F CRC64;
MAVYTEVTDD ALAAFLEGYD IGRMVAFRGI AEGVENSNYS LRTTEGDFIL TLYERRVDPA
DLPWFLGLME HLAAKSLPCP LPVRARDGAN LNPLAGRIAA ITTFLPGVWP RRPTVAHCGP
LGAAMARMHL AGEDYAPTRA NALGPQGWPP LLARCGDSGD AVRPGLTGEV RTALDATLAA
WPGALPRGHI HADLFPDNVF FLDHAISGLI DFYFAATDLY AYDIAVCLNA WCFEPDFSFN
ITKSRALLRG YQAVRPLSAA ETEALPVLCR GAAIRFLLTR LYDWINTPDD ALVTRKDPLD
YYWRLRFHLQ AGSAADYGV