ID   DHON_METGL              Reviewed;         412 AA.
AC   P37144;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Homoserine dehydrogenase;
DE            Short=HDH;
DE            EC=1.1.1.3;
GN   Name=hom;
OS   Methylobacillus glycogenes.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylobacillus.
OX   NCBI_TaxID=406;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 21371 / DSM 1760 / JCM 2853 / NCIMB 1210 / M 135-7;
RX   PubMed=8117070; DOI=10.1128/aem.60.1.111-119.1994;
RA   Motoyama H., Maki K., Anazawa H., Ishino S., Teshiba S.;
RT   "Cloning and nucleotide sequences of the homoserine dehydrogenase genes
RT   (hom) and the threonine synthase genes (thrC) of the Gram-negative obligate
RT   methylotroph Methylobacillus glycogenes.";
RL   Appl. Environ. Microbiol. 60:111-119(1994).
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}.
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; D14071; BAA40415.1; -; Genomic_DNA.
DR   AlphaFoldDB; P37144; -.
DR   SMR; P37144; -.
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; IPR045865; ACT-like_dom_sf.
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; PF01842; ACT; 1.
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   SUPFAM; SSF55021; SSF55021; 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..412
FT                   /note="Homoserine dehydrogenase"
FT                   /id="PRO_0000066699"
FT   DOMAIN          330..407
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   ACT_SITE        205
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   BINDING         9..16
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   412 AA;  44818 MW;  613A1B7FDECEF4AA CRC64;
     MKPINVGLLG IGTVGGGTYT VLTRNQEEIA RRAGRPIAIT RVADRNLELA RQVTGGKIDV
     TDDAFAIVSD PAIDIVVELI GGYTVARELV LKAIENGKHV VTANKALIAC MAMKFLPLRR
     KKASSSLLKL PLLVVSPLFK AVREGLAANR IEWIAGIING TTNFILSEMR EKGLAFADVL
     KEAQRLGYAE ADPTFDVEGI DAAHKLMILA AMLWLFVHSL CRGITKLDAV DITKRTDKGV
     ELRVHPTLIP EKRLICQCEW RNECCAGQGR CCWPTLYYGA GAGAEPTASA VADLVDGTDR
     GISCPHLAFQ PDRLVDLPIL PIGEISSAYY LRLRAVDKPG VLADVTRILG DRQISIDAMI
     QKEPQEGEDQ ADIIILTHVT VEKNMDDAIA AIEALPAISG KVTRLRMEEL SR