ID   H0BXA7_9BURK            Unreviewed;       461 AA.
AC   H0BXA7;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213};
DE            EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213};
GN   ORFNames=KYG_10020 {ECO:0000313|EMBL:EHL23163.1};
OS   Acidovorax sp. NO-1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=512030 {ECO:0000313|EMBL:EHL23163.1, ECO:0000313|Proteomes:UP000003485};
RN   [1] {ECO:0000313|EMBL:EHL23163.1, ECO:0000313|Proteomes:UP000003485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NO-1 {ECO:0000313|EMBL:EHL23163.1,
RC   ECO:0000313|Proteomes:UP000003485};
RX   PubMed=22374962; DOI=10.1128/JB.06814-11;
RA   Huang Y., Li H., Rensing C., Zhao K., Johnstone L., Wang G.;
RT   "Genome Sequence of the Facultative Anaerobic Arsenite-Oxidizing and
RT   Nitrate-Reducing Bacterium Acidovorax sp. Strain NO1.";
RL   J. Bacteriol. 194:1635-1636(2012).
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         Evidence={ECO:0000256|ARBA:ARBA00001406};
CC   -!- SIMILARITY: Belongs to the homoserine dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00006753, ECO:0000256|RuleBase:RU004171}.
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DR   EMBL; AGTS01000075; EHL23163.1; -; Genomic_DNA.
DR   RefSeq; WP_008904697.1; NZ_AGTS01000075.1.
DR   AlphaFoldDB; H0BXA7; -.
DR   STRING; 512030.KYG_10020; -.
DR   PATRIC; fig|512030.4.peg.1967; -.
DR   OrthoDB; 9808167at2; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000003485; Unassembled WGS sequence.
DR   GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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   PANTHER; PTHR43331; HOMOSERINE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43331:SF1; HOMOSERINE DEHYDROGENASE; 1.
DR   Pfam; PF00742; Homoserine_dh; 1.
DR   Pfam; PF03447; NAD_binding_3; 1.
DR   PIRSF; PIRSF000098; Homoser_dehydrog; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS01042; HOMOSER_DHGENASE; 1.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|PIRSR:PIRSR000098-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003485}.
FT   DOMAIN          31..150
FT                   /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03447"
FT   DOMAIN          158..337
FT                   /note="Homoserine dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00742"
FT   ACT_SITE        226
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000098-1"
FT   BINDING         30..37
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
FT   BINDING         126
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
FT   BINDING         211
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
SQ   SEQUENCE   461 AA;  47647 MW;  D8009749AF8F152C CRC64;
     MVRDPVPSFV EAPLLPPSAT AMRPLRVGMI GIGTVGAGTF RVLARNQGLI AGRAGRGIKL
     VVVCARSLAR AMGVVGKDVA LTNDPMQVAT HPEVDVLVEA AGGTGPARDW VLAAIRAGKH
     VVTANKALLA THGNEIFTAA RQHGVAVAYE GAVAVSIPIV KALREGLTAN RIEWVAGIIN
     GTTNFILSKM RDEGVGFAEA LAQAQALGYA EADPTFDIEG IDAAHKISLL AANAFGMPVR
     FADAQVEGIT ALQGLDVACA GQLGYRIKLL GVARRRGDEG IELRVQPALV PATHMLAHVN
     GSMNAVMVKG DASGVTMYYG AGAGGEQTAS AVIADLVDVA RLDGTHAGQR VPHLGFHPHA
     VDGQLAVLPR AKVHTRHYLR VPVHSAQQIE AVGAWLAGQH VPVLQVALAH DTALPPGTGP
     QVLVLTDAVA QATVDLAVHA LTAHTAVAGP VVALRVEVLQ G
//