ID   KHSE_CANAL              Reviewed;         357 AA.
AC   Q92209; A0A1D8PN04; Q5A523;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2017, sequence version 3.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Homoserine kinase;
DE            Short=HK;
DE            Short=HSK;
DE            EC=2.7.1.39;
GN   Name=THR1; OrderedLocusNames=CAALFM_C500650CA; ORFNames=CaO19.923;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-147.
RC   STRAIN=SS;
RA   White T.C.;
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of L-homoserine
CC       to L-homoserine phosphate. {ECO:0000250}.
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;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 4/5.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. Homoserine kinase
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP017627; AOW29508.1; -; Genomic_DNA.
DR   EMBL; U67193; AAB08101.1; -; Genomic_DNA.
DR   RefSeq; XP_716762.2; XM_711669.2.
DR   AlphaFoldDB; Q92209; -.
DR   SMR; Q92209; -.
DR   STRING; 237561.Q92209; -.
DR   GeneID; 3641572; -.
DR   KEGG; cal:CAALFM_C500650CA; -.
DR   CGD; CAL0000196189; THR1.
DR   VEuPathDB; FungiDB:C5_00650C_A; -.
DR   eggNOG; KOG1537; Eukaryota.
DR   HOGENOM; CLU_041243_2_1_1; -.
DR   InParanoid; Q92209; -.
DR   OMA; CANRIPH; -.
DR   OrthoDB; 793380at2759; -.
DR   UniPathway; UPA00050; UER00064.
DR   Proteomes; UP000000559; Chromosome 5.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004413; F:homoserine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009092; P:homoserine metabolic process; IEA:EnsemblFungi.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis; ATP-binding; Kinase; Nucleotide-binding;
KW   Reference proteome; Threonine biosynthesis; Transferase.
FT   CHAIN           1..357
FT                   /note="Homoserine kinase"
FT                   /id="PRO_0000156654"
FT   BINDING         99..109
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        4
FT                   /note="I -> T (in Ref. 4; AAB08101)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   357 AA;  39130 MW;  9F5F3BD019881D93 CRC64;
     MSVISFKIKV PASSANIGPG FDVLGIGLQL YLTITVTIDP SIDTSSDPHH ALLSYEGDGK
     VPFESNENLI TQTALYVMRC NGIKDFPRGT HIHVNNPIPL GRGLGSSASA IVAGVYLGNE
     IGNLKLDKYR LLDYCLMIER HPDNIAAAML GGFIGSYLNE LSSEDSQLTT VPLDYILPKV
     KNGELITPQD KIVSQQPPNN IGQYVEYKWN KKIKCLTIIP NFELSTDLSR SVLPKNYQLP
     DIVYNLQRIA ILTTALTQDP PNHKVIYQSM KDKLHQPYRF GLIPGLNTVL QKITPESYPG
     LCGICLSGAG PTILCLATDG FEKIANDVIE IFKQEGIECD SKLLDLAYDG ATVEYGS