ID   DHOM_METGL              Reviewed;         435 AA.
AC   P37143;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   02-SEP-2026, entry version 97.
DE   RecName: Full=Homoserine dehydrogenase;
DE            Short=HDH;
DE            Short=HSD;
DE            EC=1.1.1.3 {ECO:0000250|UniProtKB:P31116};
GN   Name=hom;
OS   Methylobacillus glycogenes.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Nitrosomonadales; Methylophilaceae; Methylobacillus.
OX   NCBI_TaxID=406;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 21276 / NCIMB 12105;
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   -!- FUNCTION: Catalyzes the conversion of L-aspartate-beta-semialdehyde (L-
CC       Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of
CC       threonine and methionine from aspartate.
CC       {ECO:0000250|UniProtKB:P31116}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-homoserine + NADP(+) = L-aspartate 4-semialdehyde + NADPH +
CC         H(+); 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         Evidence={ECO:0000250|UniProtKB:P31116};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15763;
CC         Evidence={ECO:0000250|UniProtKB:P31116};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-homoserine + NAD(+) = L-aspartate 4-semialdehyde + NADH +
CC         H(+); 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         Evidence={ECO:0000250|UniProtKB:P31116};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15759;
CC         Evidence={ECO:0000250|UniProtKB:P31116};
CC   -!- COFACTOR:
CC       Name=a metal cation; Xref=ChEBI:CHEBI:25213;
CC         Evidence={ECO:0000250|UniProtKB:P31116};
CC       Note=A sodium ion is seen in the structure; a metal ion may subtly
CC       affect the relative position of the nucleotide-binding region to
CC       influence enzyme activity, and could increase the stability of the
CC       enzyme. {ECO:0000250|UniProtKB:P31116};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-homoserine from L-aspartate: step 3/3.
CC       {ECO:0000250|UniProtKB:P31116}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 3/5. {ECO:0000250|UniProtKB:P31116}.
CC   -!- SIMILARITY: Belongs to the homoserine dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; D14070; BAA40414.1; -; Genomic_DNA.
DR   AlphaFoldDB; P37143; -.
DR   SMR; P37143; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   GO; GO:0004412; F:homoserine dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0070403; F:NAD+ binding; ISS:UniProtKB.
DR   GO; GO:0071265; P:L-methionine biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0009088; P:L-threonine biosynthetic process; ISS:UniProtKB.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 3.30.360.10; Dihydrodipicolinate Reductase, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR001342; HDH_cat.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; NF004976; PRK06349.1; 1.
DR   PANTHER; PTHR43331; HOMOSERINE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43331:SF1; HOMOSERINE DEHYDROGENASE; 1.
DR   Pfam; PF00742; Homoserine_dh; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Metal-binding; Methionine biosynthesis; NAD; NADP;
KW   Oxidoreductase; Sodium; Threonine biosynthesis.
FT   CHAIN           1..435
FT                   /note="Homoserine dehydrogenase"
FT                   /id="PRO_0000066698"
FT   REGION          255..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          377..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        262..274
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        377..391
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        204
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   BINDING         13
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000250|UniProtKB:O58802"
FT   BINDING         14
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P31116"
FT   BINDING         14
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:F9VNG5"
FT   BINDING         14
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000250|UniProtKB:O58802"
FT   BINDING         43
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:F9VNG5"
FT   BINDING         43
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000250|UniProtKB:O58802"
FT   BINDING         105
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:F9VNG5"
FT   BINDING         105
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000250|UniProtKB:O58802"
FT   BINDING         129
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000250|UniProtKB:P31116"
FT   BINDING         132
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000250|UniProtKB:P31116"
FT   BINDING         134
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000250|UniProtKB:P31116"
FT   BINDING         136
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000250|UniProtKB:P31116"
SQ   SEQUENCE   435 AA;  48227 MW;  58468B0E7A81ACAB CRC64;
     MKPINVGLLG IGTVGGGTYT VLTRNQEGNR APCRPPNCHH ARRDRNLELA RKVTGGQIDV
     TDDAFAVVVR PRHRHRGRID RRIHHRARTG YEGDRERQAR VAANKALMLA WQRDFRRVAQ
     QKGVIVAFEA AVAGGIPIIK AVAAGAGRQP SSRVLRAIIN GTTNFILSEM REKGLAFADV
     LKEAQPRLCE ATRPSTSRAW TAHKLMILAA IGFGIPMQFD KAYVEGISKL DALDIRYAEE
     LGYRQAAWHA PSAPARGVEL ARAPDPDPRE TPDRQCQRRH NAVLVSDACR SHLVYRPDAC
     RRHASAVVAD IVDGTRTAYH RRAPAVPHLL SSPTSSWTCR FAIGEVSSAY YLRLRAVDKP
     GRDGHVTRIL ATGSLHRCDD SEGNRRQAER RRSGRHHHPD HVTVEKNMDD AIVAIEALPA
     ISGSVTRLRM EELSR
//