ID   M0MC97_9EURY            Unreviewed;       317 AA.
AC   M0MC97;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213};
DE            EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213};
GN   ORFNames=C449_15372 {ECO:0000313|EMBL:EMA43371.1};
OS   Halococcus saccharolyticus DSM 5350.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halococcaceae; Halococcus.
OX   NCBI_TaxID=1227455 {ECO:0000313|EMBL:EMA43371.1, ECO:0000313|Proteomes:UP000011669};
RN   [1] {ECO:0000313|EMBL:EMA43371.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5350 {ECO:0000313|EMBL:EMA43371.1};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EMA43371.1}.
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DR   EMBL; AOMD01000030; EMA43371.1; -; Genomic_DNA.
DR   RefSeq; WP_006078932.1; NZ_AOMD01000030.1.
DR   AlphaFoldDB; M0MC97; -.
DR   STRING; 1227455.C449_15372; -.
DR   PATRIC; fig|1227455.4.peg.3127; -.
DR   InParanoid; M0MC97; -.
DR   OrthoDB; 4488at2157; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000011669; Unassembled WGS sequence.
DR   GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-EC.
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; IPR006096; Glu/Leu/Phe/Val/Trp_DH_C.
DR   InterPro; IPR001342; HDH_cat.
DR   InterPro; IPR019811; HDH_CS.
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; PF00208; ELFV_dehydrog; 1.
DR   Pfam; PF00742; Homoserine_dh; 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.
DR   PROSITE; PS01042; HOMOSER_DHGENASE; 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:UP000011669}.
FT   DOMAIN          2..57
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00208"
FT   DOMAIN          138..313
FT                   /note="Homoserine dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00742"
FT   ACT_SITE        205
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036497-1"
FT   BINDING         7..12
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
FT   BINDING         106
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
FT   BINDING         190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
SQ   SEQUENCE   317 AA;  32128 MW;  BCA41714E6F631FD CRC64;
     MKLAIVGCGA VGSAVAELAG EYGHRVTALA DSTSATVDPD GIDVGTALDR KAEGRGVGTD
     GIDRALDAEY DALVEATPTT LGDAKPGFAH VRHALDRDAH AVLANKGPVA ERYADLRAAE
     RESEGEVLFE AAVGGAIPVL STIADLGPTN VTAVRGVLNG TANFILSRMS AEGLDYGHVL
     AEAQDLGVAE ADPTFDVEGT DAALKCVILA NVLGDGETTL ADANVTGITD LTPSALDLAT
     DDGRTVRLVG EVVDGDGAPE VRVGPRLVPE NGTLAVTGTQ NIVQLETRHA GQLNLSGRGA
     GGRATATAVL GDVGRLP
//