ID A0A1I6E5U6_9RHOB Unreviewed; 433 AA.
AC A0A1I6E5U6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213};
DE EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213};
GN ORFNames=SAMN04515673_107140 {ECO:0000313|EMBL:SFR12931.1};
OS Poseidonocella sedimentorum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Poseidonocella.
OX NCBI_TaxID=871652 {ECO:0000313|EMBL:SFR12931.1, ECO:0000313|Proteomes:UP000199302};
RN [1] {ECO:0000313|EMBL:SFR12931.1, ECO:0000313|Proteomes:UP000199302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMM 9023,NRIC 0796,JCM 17311,KCTC 23692
RC {ECO:0000313|Proteomes:UP000199302};
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}.
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DR EMBL; FOYI01000007; SFR12931.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6E5U6; -.
DR STRING; 871652.SAMN04515673_107140; -.
DR OrthoDB; 9808167at2; -.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00465.
DR Proteomes; UP000199302; 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:UP000199302}.
FT DOMAIN 355..429
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 15..22
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
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; 45133 MW; 90F5B686E955F409 CRC64;
MPETHKSPPL RLGIAGLGTV GAGVVRIVRQ KAELIAARAG RPVEITAVSA RNRDKDRGVS
LEGYDWEDNP VTLARRADVD VLVELMGGSD GPAKAATEAA IAAGKDVVTA NKAMLAHHGQ
ALAEAAEAAG RVIRFEAAVA GGIPIIKSLT EGLAANEITR VMGVMNGTCN YILTRMQSAG
LPYETVFQEA DKLGYLEADP QLDVGGIDAG HKLSLLSSIA FGTQVDFDAV QLEGIGKIMI
EDIEQAADLG YRIKLLGVAQ LTGRGLEQRM SPCLVPATSP LGQLEGGTNM VVVEGDDVGQ
IVLRGAGAGE GPTASAVMGD VMDIARGLRI STFGQPASTL KTAQPASGNT PAPYYLRMTL
HDKPGALAKV AARLGDAGVS IDRMRQYGHD DTAAPVLIIT HKTTRGALDE AIAAIETLNV
VTDTPVALRI EEV
//
