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Database: UniProt
Entry: A0A1I6PN39_9RHOB
LinkDB: A0A1I6PN39_9RHOB
Original site: A0A1I6PN39_9RHOB 
ID   A0A1I6PN39_9RHOB        Unreviewed;       433 AA.
AC   A0A1I6PN39;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213};
DE            EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213};
GN   ORFNames=SAMN04488040_0250 {ECO:0000313|EMBL:SFS41540.1};
OS   Sulfitobacter marinus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Sulfitobacter.
OX   NCBI_TaxID=394264 {ECO:0000313|EMBL:SFS41540.1, ECO:0000313|Proteomes:UP000199239};
RN   [1] {ECO:0000313|Proteomes:UP000199239}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23422 {ECO:0000313|Proteomes:UP000199239};
RA   Varghese N., Submissions S.;
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}.
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DR   EMBL; FPAJ01000001; SFS41540.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6PN39; -.
DR   STRING; 394264.SAMN04488040_0250; -.
DR   OrthoDB; 9808167at2; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000199239; 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; 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.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|PIRSR:PIRSR000098-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199239}.
FT   DOMAIN          355..433
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   ACT_SITE        212
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000098-1"
FT   BINDING         112
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
FT   BINDING         197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
SQ   SEQUENCE   433 AA;  44981 MW;  533CAA78CC8333D8 CRC64;
     MSHPLQSGPL RLGIAGLGTV GVGVVRILRK QADLLEARTG RKITISAVSA RSKDKDRGVN
     LSGYAWEDDP VALAKRDDVD VFVELIGGDE GPAKDATEAA LGAGKDVVTA NKAMLAIHGQ
     SLAEQAEAAG RHIRYEAAVA GGIPVIKVLN EALAGNEITR VMGVMNGSCN YILTRMEDAG
     LPYEDVFAEA DGLGYLEADP ALDVGGIDAA HKLAILSSIA FGSRVDFDGI DLEGIERVSI
     EDIRAAAGMG YKIKLLGVAQ MTGRGLEQRM QPCLVPDTSP LGQLSGGTNM IVLEGDAVGQ
     IVLRGPGAGE GPTASAVLSD ICDLARGWQG PVFGQKASTL TNTASAMSQA PAAFYLRMGL
     LDKPGALAKV ATVLGEAGIS IDRMRQTAHH NDHAPVLIVT HKTTRSALDD ALAAMAKTGV
     LASDPVALRI EDL
//
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