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Database: UniProt
Entry: A0A078KE29_9GAMM
LinkDB: A0A078KE29_9GAMM
Original site: A0A078KE29_9GAMM 
ID   A0A078KE29_9GAMM        Unreviewed;       432 AA.
AC   A0A078KE29;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213};
DE            EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213};
GN   Name=hom {ECO:0000313|EMBL:CDZ16297.1};
GN   ORFNames=CEM_025 {ECO:0000313|EMBL:CDZ16297.1};
OS   Candidatus Evansia muelleri.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Zymobacter group; Evansia.
OX   NCBI_TaxID=1495769 {ECO:0000313|EMBL:CDZ16297.1, ECO:0000313|Proteomes:UP000032420};
RN   [1] {ECO:0000313|Proteomes:UP000032420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Santos-Garcia D.;
RL   Submitted (JUL-2014) 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-homoserine + NADP(+) = H(+) + L-aspartate 4-semialdehyde +
CC         NADPH; 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:0000256|ARBA:ARBA00000116};
CC   -!- SIMILARITY: Belongs to the homoserine dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00006753}.
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DR   EMBL; LM655252; CDZ16297.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A078KE29; -.
DR   STRING; 1495769.CEM_025; -.
DR   KEGG; eme:CEM_025; -.
DR   PATRIC; fig|1495769.3.peg.19; -.
DR   HOGENOM; CLU_009116_1_0_6; -.
DR   OrthoDB; 9808167at2; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000032420; 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; 3.30.70.260; -; 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; 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.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|PIRSR:PIRSR000098-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:CDZ16297.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032420}.
FT   DOMAIN          13..129
FT                   /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03447"
FT   DOMAIN          137..315
FT                   /note="Homoserine dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00742"
FT   ACT_SITE        205
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000098-1"
FT   BINDING         105
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
FT   BINDING         190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
SQ   SEQUENCE   432 AA;  48217 MW;  8625747791F6C6B9 CRC64;
     MIILTPVKIG ICGLGTVGIG TFNVLKRNIN KIVYSAGKKI IIEQICACKT LFNKINFINK
     TNNIFDIVYN HNIDIVVELI GGCNIALKFV IESIKNGKHV VTANKYMIAN YGTDIFSLAN
     KKGVIVAFEA AVAGGIPIIK SLREGLVANS IKWLIGILNG TLNYILTSMH NEYKSFKKIL
     LKAKLLGYAE FNHILDIEGI DVAHKLVILA SIAYCIPLKI HQIYIEGISK IISDDIIYAD
     KLGYKIKHLG ISIINKYGLE LRVHPTMIKK TCLISNINDI NNAIEIMGDA VGSNFYSGIG
     AGSEPTASSI ISDLINITSY INIKKKISFK DYIEKNIKIL SMDNIITAYY LRIIASYPKY
     DLLSKIFEIF NVNKISIKSI YKKYIISKKL INIIIITNLV KELNMNISIN NIELLDNVIN
     SVYIRIGYLN NN
//
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