ID   A0A0K1NG87_9BURK        Unreviewed;       440 AA.
AC   A0A0K1NG87;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213};
DE            EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213};
GN   ORFNames=ADJ79_11620 {ECO:0000313|EMBL:AKU67706.1};
OS   Ottowia sp. oral taxon 894.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Ottowia.
OX   NCBI_TaxID=1658672 {ECO:0000313|EMBL:AKU67706.1, ECO:0000313|Proteomes:UP000056623};
RN   [1] {ECO:0000313|Proteomes:UP000056623}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W10237 {ECO:0000313|Proteomes:UP000056623};
RA   Holder M.E., Ajami N.J., Petrosino J.F.;
RL   Submitted (JUL-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, ECO:0000256|RuleBase:RU004171}.
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DR   EMBL; CP012073; AKU67706.1; -; Genomic_DNA.
DR   RefSeq; WP_050716093.1; NZ_CP012073.1.
DR   AlphaFoldDB; A0A0K1NG87; -.
DR   STRING; 1658672.ADJ79_11620; -.
DR   KEGG; oto:ADJ79_11620; -.
DR   PATRIC; fig|1658672.3.peg.2930; -.
DR   OrthoDB; 9808167at2; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000056623; 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   CDD; cd04881; ACT_HSDH-Hom; 1.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
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; PF01842; ACT; 1.
DR   Pfam; PF00742; Homoserine_dh; 1.
DR   Pfam; PF03447; NAD_binding_3; 1.
DR   PIRSF; PIRSF000098; Homoser_dehydrog; 1.
DR   SUPFAM; SSF55021; ACT-like; 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; PS51671; ACT; 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   ECO:0000313|EMBL:AKU67706.1}.
FT   DOMAIN          356..435
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   ACT_SITE        205
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000098-1"
FT   BINDING         9..16
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
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   440 AA;  46999 MW;  6DC309BAC40DA601 CRC64;
     MQAIQVGLLG IGTVGSGTFN VLRRNQEEIK RRAGRGIEIV MVADLDTQRA RQIVGPDVQV
     VADAREVIAN PDIEIVVELI GGYGVARTLV LEAIAAGKHV VTANKALLAV HGTEIFEAAQ
     KKGVMVAFEA AVAGGIPIIK ALREGLTANR IQWLAGIING TTNFILSEMR DKGLDFDVAL
     KEAQRLGYAE ADPTFDIEGI DAAHKATLMS AIAFGIPVQF DRAYVEGITQ LAAADIQYAE
     QLGYRIKLLG MSKRREGEGV ELRVHPTLIP ARRLIANVEG AMNAVLVQGD AVGATLHYGK
     GAGSEPTASA VIADLVDVTR LATSDPQHRV PHLAFQPGAL RHVQVLPIEQ VITSYYLRLR
     VKDETGVLAQ VTRILADAGI SINAVLQRGT GSAAQNAHET DLIILTHNAL EGSMNAALAR
     LQQLPAVLAP IVRIRKEELA
//