KHSE_ECOLI
ID KHSE_ECOLI Reviewed; 310 AA.
AC P00547;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Homoserine kinase;
DE Short=HK;
DE Short=HSK;
DE EC=2.7.1.39;
GN Name=thrB; OrderedLocusNames=b0003, JW0002;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6259626; DOI=10.1093/nar/9.2.339;
RA Cossart P., Katinka M., Yaniv M.;
RT "Nucleotide sequence of the thrB gene of E. coli, and its two adjacent
RT regions; the thrAB and thrBC junctions.";
RL Nucleic Acids Res. 9:339-347(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION TO 166-190.
RA Deborde D.C., Strange J.C., Wright B.E.;
RT "Update on the nucleotide sequence of the thrB gene of E. coli.";
RL Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP FUNCTION AS A HOMOSERINE KINASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP KINETIC PARAMETERS, AND MUTAGENESIS OF HIS-139; HIS-203; HIS-206 AND
RP ARG-235.
RX PubMed=8973190; DOI=10.1021/bi962203z;
RA Huo X., Viola R.E.;
RT "Substrate specificity and identification of functional groups of
RT homoserine kinase from Escherichia coli.";
RL Biochemistry 35:16180-16185(1996).
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of L-homoserine
CC to L-homoserine phosphate. Is also able to phosphorylate the hydroxy
CC group on gamma-carbon of L-homoserine analogs when the functional group
CC at the alpha-position is a carboxyl, an ester, or even a hydroxymethyl
CC group. Neither L-threonine nor L-serine are substrates of the enzyme.
CC {ECO:0000269|PubMed:8973190}.
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:0000269|PubMed:8973190};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.14 mM for L-homoserine {ECO:0000269|PubMed:8973190};
CC KM=31.8 mM for D-homoserine {ECO:0000269|PubMed:8973190};
CC KM=0.13 mM for ATP {ECO:0000269|PubMed:8973190};
CC Note=The catalytic efficiency is 500-fold higher with L-homoserine
CC than with D-homoserine as substrate.;
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 4/5.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. Homoserine kinase
CC subfamily. {ECO:0000305}.
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DR EMBL; L13601; AAA20618.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97302.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73114.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96580.2; -; Genomic_DNA.
DR PIR; S56630; KIECM.
DR RefSeq; NP_414544.1; NC_000913.3.
DR RefSeq; WP_000241662.1; NZ_LN832404.1.
DR AlphaFoldDB; P00547; -.
DR SMR; P00547; -.
DR BioGRID; 4261934; 9.
DR IntAct; P00547; 2.
DR STRING; 511145.b0003; -.
DR BindingDB; P00547; -.
DR SWISS-2DPAGE; P00547; -.
DR jPOST; P00547; -.
DR PaxDb; P00547; -.
DR PRIDE; P00547; -.
DR EnsemblBacteria; AAC73114; AAC73114; b0003.
DR EnsemblBacteria; BAB96580; BAB96580; BAB96580.
DR GeneID; 947498; -.
DR KEGG; ecj:JW0002; -.
DR KEGG; eco:b0003; -.
DR PATRIC; fig|1411691.4.peg.2280; -.
DR EchoBASE; EB0992; -.
DR eggNOG; COG0083; Bacteria.
DR HOGENOM; CLU_041243_1_1_6; -.
DR InParanoid; P00547; -.
DR OMA; CANRIPH; -.
DR PhylomeDB; P00547; -.
DR BioCyc; EcoCyc:HOMOSERKIN-MON; -.
DR BioCyc; MetaCyc:HOMOSERKIN-MON; -.
DR UniPathway; UPA00050; UER00064.
DR PRO; PR:P00547; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004413; F:homoserine kinase activity; IDA:EcoCyc.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009088; P:threonine biosynthetic process; IMP:EcoCyc.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.890; -; 1.
DR HAMAP; MF_00384; Homoser_kinase; 1.
DR InterPro; IPR013750; GHMP_kinase_C_dom.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR006203; GHMP_knse_ATP-bd_CS.
DR InterPro; IPR000870; Homoserine_kinase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR Pfam; PF08544; GHMP_kinases_C; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR PIRSF; PIRSF000676; Homoser_kin; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55060; SSF55060; 1.
DR TIGRFAMs; TIGR00191; thrB; 1.
DR PROSITE; PS00627; GHMP_KINASES_ATP; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; ATP-binding; Cytoplasm; Kinase;
KW Nucleotide-binding; Reference proteome; Threonine biosynthesis;
KW Transferase.
FT CHAIN 1..310
FT /note="Homoserine kinase"
FT /id="PRO_0000156567"
FT BINDING 91..101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 139
FT /note="H->L: 35-fold decrease in kinase activity."
FT /evidence="ECO:0000269|PubMed:8973190"
FT MUTAGEN 203
FT /note="H->L: 2-fold decrease in kinase activity but nearly
FT no change in substrates affinity."
FT /evidence="ECO:0000269|PubMed:8973190"
FT MUTAGEN 206
FT /note="H->Q: 3500-fold decrease in kinase activity."
FT /evidence="ECO:0000269|PubMed:8973190"
FT MUTAGEN 235
FT /note="R->H: 250-fold decrease in kinase activity but no
FT change in substrates affinity."
FT /evidence="ECO:0000269|PubMed:8973190"
FT MUTAGEN 235
FT /note="R->L: 26200-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:8973190"
SQ SEQUENCE 310 AA; 33624 MW; 0F225F9F1B634BE8 CRC64;
MVKVYAPASS ANMSVGFDVL GAAVTPVDGA LLGDVVTVEA AETFSLNNLG RFADKLPSEP
RENIVYQCWE RFCQELGKQI PVAMTLEKNM PIGSGLGSSA CSVVAALMAM NEHCGKPLND
TRLLALMGEL EGRISGSIHY DNVAPCFLGG MQLMIEENDI ISQQVPGFDE WLWVLAYPGI
KVSTAEARAI LPAQYRRQDC IAHGRHLAGF IHACYSRQPE LAAKLMKDVI AEPYRERLLP
GFRQARQAVA EIGAVASGIS GSGPTLFALC DKPETAQRVA DWLGKNYLQN QEGFVHICRL
DTAGARVLEN
