KHSE_YEAST
ID KHSE_YEAST Reviewed; 357 AA.
AC P17423; D3DKX2;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Homoserine kinase;
DE Short=HK;
DE Short=HSK;
DE EC=2.7.1.39 {ECO:0000269|PubMed:2165904};
GN Name=THR1; OrderedLocusNames=YHR025W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-16, FUNCTION,
RP CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=2165904; DOI=10.1111/j.1432-1033.1990.tb19100.x;
RA Mannhaupt G., Pohlenz H.D., Seefluth A.K., Pilz U., Feldmann H.;
RT "Yeast homoserine kinase. Characteristics of the corresponding gene, THR1,
RT and the purified enzyme, and evolutionary relationships with other enzymes
RT of threonine metabolism.";
RL Eur. J. Biochem. 191:115-122(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2176637; DOI=10.1016/0378-1119(90)90250-u;
RA Schultes N.P., Ellington A.D., Cherry J.M., Szostak J.W.;
RT "Saccharomyces cerevisiae homoserine kinase is homologous to prokaryotic
RT homoserine kinases.";
RL Gene 96:177-180(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-133, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of L-homoserine
CC to L-homoserine phosphate in the threonine biosynthesis pathway.
CC {ECO:0000269|PubMed:2165904}.
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:2165904};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13986;
CC Evidence={ECO:0000305|PubMed:2165904};
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 4/5. {ECO:0000305|PubMed:2165904}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:2165904}.
CC -!- MISCELLANEOUS: Present with 92600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. Homoserine kinase
CC subfamily. {ECO:0000305}.
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DR EMBL; X52901; CAA37083.1; -; Genomic_DNA.
DR EMBL; M37692; AAA35154.1; -; Genomic_DNA.
DR EMBL; U10399; AAB68871.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06716.1; -; Genomic_DNA.
DR PIR; S46772; S46772.
DR RefSeq; NP_011890.1; NM_001179155.1.
DR AlphaFoldDB; P17423; -.
DR SMR; P17423; -.
DR BioGRID; 36456; 119.
DR DIP; DIP-4305N; -.
DR IntAct; P17423; 8.
DR MINT; P17423; -.
DR STRING; 4932.YHR025W; -.
DR iPTMnet; P17423; -.
DR MaxQB; P17423; -.
DR PaxDb; P17423; -.
DR PRIDE; P17423; -.
DR EnsemblFungi; YHR025W_mRNA; YHR025W; YHR025W.
DR GeneID; 856420; -.
DR KEGG; sce:YHR025W; -.
DR SGD; S000001067; THR1.
DR VEuPathDB; FungiDB:YHR025W; -.
DR eggNOG; KOG1537; Eukaryota.
DR HOGENOM; CLU_041243_2_1_1; -.
DR InParanoid; P17423; -.
DR OMA; CANRIPH; -.
DR BioCyc; YEAST:YHR025W-MON; -.
DR UniPathway; UPA00050; UER00064.
DR PRO; PR:P17423; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P17423; protein.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004413; F:homoserine kinase activity; IDA:SGD.
DR GO; GO:0009092; P:homoserine metabolic process; IDA:SGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009088; P:threonine biosynthetic process; IMP:SGD.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.890; -; 1.
DR HAMAP; MF_00384; Homoser_kinase; 1.
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; 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; Direct protein sequencing;
KW Isopeptide bond; Kinase; Nucleotide-binding; Reference proteome;
KW Threonine biosynthesis; Transferase; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2165904"
FT CHAIN 2..357
FT /note="Homoserine kinase"
FT /id="PRO_0000156656"
FT BINDING 104..114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CROSSLNK 133
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 87
FT /note="Missing (in Ref. 1; CAA37083)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 357 AA; 38712 MW; 1C1A951E00550ECB CRC64;
MVRAFKIKVP ASSANIGPGY DVLGVGLSLF LELDVTIDSS QAQETNDDPN NCKLSYTKES
EGYSTVPLRS DANLITRTAL YVLRCNNIRN FPSGTKVHVS NPIPLGRGLG SSGAAVVAGV
ILGNEVAQLG FSKQRMLDYC LMIERHPDNI TAAMMGGFCG SFLRDLTPQE VERREIPLAE
VLPEPSGGED TGLVPPLPPT DIGRHVKYQW NPAIKCIAII PQFELSTADS RGVLPKAYPT
QDLVFNLQRL AVLTTALTMD PPNADLIYPA MQDRVHQPYR KTLIPGLTEI LSCVTPSTYP
GLLGICLSGA GPTILALATE NFEEISQEII NRFAKNGIKC SWKLLEPAYD GASVEQQ
