KHSE_NITEC
ID KHSE_NITEC Reviewed; 316 AA.
AC Q0AHY7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=Neut_0775;
OS Nitrosomonas eutropha (strain DSM 101675 / C91 / Nm57).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=335283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 101675 / C91 / Nm57;
RX PubMed=17991028; DOI=10.1111/j.1462-2920.2007.01409.x;
RA Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S.,
RA Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M., Wei X.;
RT "Whole-genome analysis of the ammonia-oxidizing bacterium, Nitrosomonas
RT eutropha C91: implications for niche adaptation.";
RL Environ. Microbiol. 9:2993-3007(2007).
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; CP000450; ABI59045.1; -; Genomic_DNA.
DR RefSeq; WP_011633870.1; NC_008344.1.
DR AlphaFoldDB; Q0AHY7; -.
DR SMR; Q0AHY7; -.
DR STRING; 335283.Neut_0775; -.
DR EnsemblBacteria; ABI59045; ABI59045; Neut_0775.
DR KEGG; net:Neut_0775; -.
DR eggNOG; COG2334; Bacteria.
DR HOGENOM; CLU_053300_0_0_4; -.
DR OMA; DPTHFER; -.
DR OrthoDB; 1003984at2; -.
DR UniPathway; UPA00050; UER00064.
DR Proteomes; UP000001966; 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 Threonine biosynthesis; Transferase.
FT CHAIN 1..316
FT /note="Homoserine kinase"
FT /id="PRO_1000022584"
SQ SEQUENCE 316 AA; 35554 MW; 2BBA1B1AEF425089 CRC64;
MSVFTPVTKK QLAVWLQNYS LGSLTDLQGI SSGIENTNYF VTTTQGKFIL TLFEKLTSTE
LPFYLNLMAY LSEQGIPCPK PIESQDHALL GTLNGKPASI VSFLPGQSMT QIREEQCAQV
GEILAKMHLA GLNYNGKNRN PRGLDWWQTA AGTVMPFLSR SEQSLLDEEL QFQIKQRTTN
LPQGIIHADL FRDNVLFTST GIGGIIDFYF ACNDALLYDL AITANDWCTL GDGVMDKARM
HALVKAYQAA RPLTAEEYPA WPAMLRAGAL RFWLSRLYDY YLPRPGELTH KKDPEYFRKI
LEYHLTNPSV LPSLQA