ID   DHOM_LACLA              Reviewed;         428 AA.
AC   Q9CGD8;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Homoserine dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.3;
GN   Name=hom; OrderedLocusNames=LL1159; ORFNames=L0090;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
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   -!- SIMILARITY: Belongs to the homoserine dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AE005176; AAK05257.1; -; Genomic_DNA.
DR   PIR; G86769; G86769.
DR   RefSeq; NP_267315.1; NC_002662.1.
DR   RefSeq; WP_003132116.1; NC_002662.1.
DR   AlphaFoldDB; Q9CGD8; -.
DR   SMR; Q9CGD8; -.
DR   STRING; 272623.L0090; -.
DR   PaxDb; Q9CGD8; -.
DR   EnsemblBacteria; AAK05257; AAK05257; L0090.
DR   KEGG; lla:L0090; -.
DR   PATRIC; fig|272623.7.peg.1239; -.
DR   eggNOG; COG0460; Bacteria.
DR   HOGENOM; CLU_009116_1_0_9; -.
DR   OMA; LMFYGPG; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000002196; Chromosome.
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   Reference proteome; Threonine biosynthesis.
FT   CHAIN           1..428
FT                   /note="Homoserine dehydrogenase"
FT                   /id="PRO_0000066696"
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;  46921 MW;  B99C159FB1BEF21C CRC64;
     MTVNIAILGF GTVGTGLPTL ISENKEKLSK ILDEEIVISK VLMRDEKAIE KARAQGYQYD
     FVLTLEEILA DSEISIVVEL MGRIEPAKTY ITKVIKAGKN VVTANKDLLA VHGTELRALA
     EKHHVALYYE AAVAGGIPIL RTLANSFSSD KITHLLGILN GTSNFMMTKM SEEAWTYDQS
     LAKAQELGYA ESDPTNDVDG IDASYKLAIL SEFAFGMTLS PDQISKSGLR TIQKTDVEIA
     QQFGYVLKLT GEINEVESGI FAEVSPTFLP KSHPLASVNG VMNAVFIESD GIGDSMFYGA
     GAGQKPTATS VLADIVRIVK REKDGTIGKS FNEYARPTSL ANPHDIVNKY YFSVETPDST
     GQLLRLVELF TSEDVSFEQV LQQKGDGHRA VVVIISHQIN RVQLLAIQDK LKEEVDFKLL
     NYFKVLGD