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Database: UniProt
Entry: A0A1H6XPU2_9BURK
LinkDB: A0A1H6XPU2_9BURK
Original site: A0A1H6XPU2_9BURK 
ID   A0A1H6XPU2_9BURK        Unreviewed;       440 AA.
AC   A0A1H6XPU2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213};
DE            EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213};
GN   ORFNames=SAMN05518853_1011311 {ECO:0000313|EMBL:SEJ31101.1};
OS   Variovorax sp. OK202.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1884311 {ECO:0000313|EMBL:SEJ31101.1, ECO:0000313|Proteomes:UP000199192};
RN   [1] {ECO:0000313|EMBL:SEJ31101.1, ECO:0000313|Proteomes:UP000199192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK202 {ECO:0000313|EMBL:SEJ31101.1,
RC   ECO:0000313|Proteomes:UP000199192};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNZJ01000001; SEJ31101.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6XPU2; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000199192; Unassembled WGS sequence.
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}.
FT   DOMAIN          355..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;  46562 MW;  12F7CE4C48A4ECFF CRC64;
     MKPIQVGLLG AGTVGSGTFK VLQRNQEEIK RRAGRGIEIT MVADLDTARA REVAGEGVKV
     VADAREIIAN PDIDIVIELI GGYGIAKQLV LEAIAAGKHV VTANKALLAV HGTEIFAAAH
     AKGVMVAFEA AVAGGIPIIK ALREGLTANS IQWLAGIING TTNFILSEMR DKGLDFATVL
     KEAQRLGYAE ADPTFDIEGV DAGHKVTLMS AIAFGIPVQF DKAHIEGITK LAAQDIKYAE
     QLGYRIKLLG VTKRTAKGIE LRVHPSLVPS KRLLANVEGA MNAVVVHGDA VGTTLYYGKG
     AGSEPTASAV IADLVDITRL HTADAAHRVP HLAFHPDAMS DLKVLPMSEV VTSYYLRLRV
     ADQAGVLAKV TGLLATAGIS IDAVLQREAD EVGGEGSTQT DLIILTHDAR EGTVNDVMAE
     LQALPTVLEP IVRIRKEELS
//
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