ID   DHOM_LACLC              Reviewed;         428 AA.
AC   P52985;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Homoserine dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.3;
GN   Name=hom;
OS   Lactococcus lactis subsp. cremoris (Streptococcus cremoris).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1359;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC   STRAIN=MG1614;
RX   PubMed=8682767; DOI=10.1128/jb.178.13.3689-3694.1996;
RA   Madsen S.M., Albrechtsen B., Hansen E.B., Israelsen H.;
RT   "Cloning and transcriptional analysis of two threonine biosynthetic genes
RT   from Lactococcus lactis MG1614.";
RL   J. Bacteriol. 178:3689-3694(1996).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-homoserine + NADP(+) = H(+) + L-aspartate 4-semialdehyde +
CC         NADPH; Xref=Rhea:RHEA:15761, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.1.1.3;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde +
CC         NADH; Xref=Rhea:RHEA:15757, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:537519; EC=1.1.1.3;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-homoserine from L-aspartate: step 3/3.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 3/5.
CC   -!- DISRUPTION PHENOTYPE: Mutant containing a deletion in both hom and thrB
CC       is unable to grow in a defined medium lacking threonine.
CC       {ECO:0000269|PubMed:8682767}.
CC   -!- SIMILARITY: Belongs to the homoserine dehydrogenase family.
CC       {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; X96988; CAA65713.1; -; Genomic_DNA.
DR   PIR; JC6049; JC6049.
DR   RefSeq; WP_011835205.1; NZ_LITG01000003.1.
DR   AlphaFoldDB; P52985; -.
DR   SMR; P52985; -.
DR   OMA; LMFYGPG; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR   InterPro; IPR016204; HDH.
DR   InterPro; IPR001342; HDH_cat.
DR   InterPro; IPR019811; HDH_CS.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00742; Homoserine_dh; 1.
DR   Pfam; PF03447; NAD_binding_3; 1.
DR   PIRSF; PIRSF000098; Homoser_dehydrog; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS01042; HOMOSER_DHGENASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Isoleucine biosynthesis; Methionine biosynthesis; NADP; Oxidoreductase;
KW   Threonine biosynthesis.
FT   CHAIN           1..428
FT                   /note="Homoserine dehydrogenase"
FT                   /id="PRO_0000066697"
FT   DOMAIN          351..425
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   ACT_SITE        206
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   BINDING         8..15
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         106
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   428 AA;  46629 MW;  B178CF30D62A6349 CRC64;
     MAVNIAILGF GTVGTGLPTL LSENKEKLAK ILDEEIVISK VLMRDNKAIE KARSQGFNYD
     FVLNLDDILA DSEISIVVEL MGRIEPAKTY ITQAIEAGKN VVTANKDLLA VHGVELRSLA
     QKHHVALYYE AAVAGGIPIL RTLANSFSSD KITHLLGILN GTSNFMMTKM SEEGWTYDES
     LAKAQELGYA ESDPTNDVDG IDASYKLAIL SEFAFGMTLA PDDIAKSGLR SIQKTDVEIA
     QQFGYVLKLT GEINEVDSGI FAEVSPTFLP KSHPLASVNG VMNAVFIESE GIGDSVFYGA
     GAGQKPTATS VLADIVRIVK RVKDGTIGKS FNEYARSTSL ANPHDIENKY YFSVETPDST
     GQLLLLVELF TSENVSFEQV LQQKGNGKRA VVVIISHKIN RVQLSAIQDK LNQEKDFKLL
     NRFKVLGD