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Database: UniProt
Entry: A0A0F7JPY4_9DEIO
LinkDB: A0A0F7JPY4_9DEIO
Original site: A0A0F7JPY4_9DEIO 
ID   A0A0F7JPY4_9DEIO        Unreviewed;       320 AA.
AC   A0A0F7JPY4;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213};
DE            EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213};
GN   ORFNames=SY84_13185 {ECO:0000313|EMBL:AKH17822.1};
OS   Deinococcus soli (ex Cha et al. 2016).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=1309411 {ECO:0000313|EMBL:AKH17822.1, ECO:0000313|Proteomes:UP000034024};
RN   [1] {ECO:0000313|EMBL:AKH17822.1, ECO:0000313|Proteomes:UP000034024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N5 {ECO:0000313|EMBL:AKH17822.1,
RC   ECO:0000313|Proteomes:UP000034024};
RA   Kim M.K., Srinivasan S., Lee J.-J.;
RT   "Deinococcus soli/N5/whole genome sequencing.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP011389; AKH17822.1; -; Genomic_DNA.
DR   RefSeq; WP_046844389.1; NZ_CP011389.1.
DR   AlphaFoldDB; A0A0F7JPY4; -.
DR   KEGG; dch:SY84_13185; -.
DR   PATRIC; fig|1309411.5.peg.2676; -.
DR   OrthoDB; 9808167at2; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000034024; Chromosome.
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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR   InterPro; IPR001342; HDH_cat.
DR   InterPro; IPR022697; HDH_short.
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; PIRSF036497; HDH_short; 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   NADP {ECO:0000256|PIRSR:PIRSR036497-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034024}.
FT   DOMAIN          10..114
FT                   /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03447"
FT   DOMAIN          130..307
FT                   /note="Homoserine dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00742"
FT   ACT_SITE        197
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036497-1"
FT   BINDING         10..15
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
FT   BINDING         100
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
FT   BINDING         182
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
SQ   SEQUENCE   320 AA;  34270 MW;  144301DC5EED36DB CRC64;
     MRTVTVGVLG CGTVGQDVLN LIWRREAIFA DLGVRIEVAG VLVRDTSRPR ACPPGTPLTT
     DPGFLQECGV VIEAMGGVEH PMSLLRPHLR SGRPVITANK ALLAEKWDEL RDYALDGKLY
     YEASVMAGTP VIGPMSTVLR ASTFQRLQAV LNGTCLYIVT QMEQGKEYAQ ALAEAQALGY
     AEDPPTLDVG GFDTAHKLTV LARFCADGNF PYDRVQVQGI EGLTLADVQA ARARGERIKL
     VAELERVNGE WQARVSPQSL PEDHPLCNAG ASRNAMVYEG EECGTLVFAG GGAGGMVTAS
     AMVGDLLDWV IGFPGHVPLH
//
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