ID   A0A0M0BZS7_9ARCH        Unreviewed;       341 AA.
AC   A0A0M0BZS7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213};
DE            EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213};
GN   ORFNames=AC479_02635 {ECO:0000313|EMBL:KON33939.1};
OS   miscellaneous Crenarchaeota group-6 archaeon AD8-1.
OC   Archaea; Candidatus Bathyarchaeota; Candidatus Bathyarchaeia.
OX   NCBI_TaxID=1685126 {ECO:0000313|EMBL:KON33939.1, ECO:0000313|Proteomes:UP000037259};
RN   [1] {ECO:0000313|EMBL:KON33939.1, ECO:0000313|Proteomes:UP000037259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AD8-1 {ECO:0000313|EMBL:KON33939.1};
RA   Lazar C.S., Baker B.J., Seitz K.W., Hyde A.S., Dick G.J., Hinrichs K.-U.,
RA   Teske A.P.;
RT   "New insights into the roles of widespread benthic archaea in carbon and
RT   nitrogen cycling.";
RL   Submitted (JUN-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}.
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:KON33939.1}.
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DR   EMBL; LFWW01000010; KON33939.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M0BZS7; -.
DR   STRING; 1685126.AC479_02635; -.
DR   PATRIC; fig|1685126.3.peg.316; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000037259; 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}.
FT   DOMAIN          4..111
FT                   /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT                   dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00208"
FT   DOMAIN          157..329
FT                   /note="Homoserine dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00742"
FT   ACT_SITE        225
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         125
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
FT   BINDING         210
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
SQ   SEQUENCE   341 AA;  36904 MW;  1B74F85BD2ABE06D CRC64;
     MRIILTGYGV VGQSLIDIFE NQKFENLKKY GFNPKVVAIT DRGGAAVNKK GLDLERIKKV
     KTREGSVAAD KKFGQPQAIA QSIIQSTEAE IMIEATSTNV VNAEPGLSNI KTAFNSGKHV
     ITTNKGPLAL AFPTLTELAD HNKVLLRFSG TVGGGTPILE FAKKCLSGDK INEMQGILNG
     TTNYILTEMA EKRVTFKKAL ELAQKLGYAE TDPSMDINGI DAACKVVIIG NWIFNKKFTL
     KDVKVNGIKN ITLKELNNAT KKGKRIKLIG SINGKPTVAP KEIRRNDPLC VSGVLNAVTF
     ISEYAGKQTI IGRGAGGIET AGAILRDLLD IKYNLANRML L
//