ID A0A1I2Y7U8_9RHOB Unreviewed; 438 AA.
AC A0A1I2Y7U8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213};
DE EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213};
GN ORFNames=SAMN04488021_103107 {ECO:0000313|EMBL:SFH21702.1};
OS Paracoccus aminovorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=34004 {ECO:0000313|EMBL:SFH21702.1, ECO:0000313|Proteomes:UP000183635};
RN [1] {ECO:0000313|EMBL:SFH21702.1, ECO:0000313|Proteomes:UP000183635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8537 {ECO:0000313|EMBL:SFH21702.1,
RC ECO:0000313|Proteomes:UP000183635};
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; FOPU01000003; SFH21702.1; -; Genomic_DNA.
DR RefSeq; WP_074966241.1; NZ_LN832559.1.
DR AlphaFoldDB; A0A1I2Y7U8; -.
DR STRING; 34004.SAMN04488021_103107; -.
DR OrthoDB; 9808167at2; -.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00465.
DR Proteomes; UP000183635; 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:UP000183635}.
FT DOMAIN 358..438
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT ACT_SITE 215
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-1"
FT BINDING 115
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
SQ SEQUENCE 438 AA; 46035 MW; DBC33A2194517507 CRC64;
MSAQNQGQNA SPLRLGIAGL GTVGIGTVKI IQKHAALLSQ RAGRPIAITA VSARDRMKNR
DADLSGYGWE EDARALAQRE DVDVFVELIG GDEGVAREAV TAALKAGKDV VTANKALLAI
HGQELAELAE AHGRVIRFEA AVAGGIPVIK AMTESLAGNE IRRVMGVMNG TCNYILTRME
NAGLPYEEVF EEARQLGYLE ADPTLDVGGI DASHKLAILA AIAFGTRPSF DAVEIEGIER
VSIDDIRRAA DMGYRIKLLG VAQMTGRGLE QRMSPCLVPA DSPLGQLQGG TNMVVIEGDS
VGQIVLRGAG AGEGPTASAV MSDVVEIARG VRMPSFGQPA LALARPQPAR TAVPAAYYIR
LALTDKPGAL AKVASVLGDS GISIDRMRQY GHQQTAGVAP VLIVTHKTTP EAIDHAIEAL
PKTGVIAGEP VELRIEEV
//
