ID A0A1F5G760_9BACT Unreviewed; 420 AA.
AC A0A1F5G760;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-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};
DE Flags: Fragment;
GN ORFNames=A3D04_02240 {ECO:0000313|EMBL:OGD87664.1};
OS Candidatus Curtissbacteria bacterium RIFCSPHIGHO2_02_FULL_40_16b.
OC Bacteria; Candidatus Curtissbacteria.
OX NCBI_TaxID=1797714 {ECO:0000313|EMBL:OGD87664.1, ECO:0000313|Proteomes:UP000177369};
RN [1] {ECO:0000313|EMBL:OGD87664.1, ECO:0000313|Proteomes:UP000177369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGD87664.1}.
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DR EMBL; MFBD01000045; OGD87664.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5G760; -.
DR STRING; 1797714.A3D04_02240; -.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00465.
DR Proteomes; UP000177369; 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}.
FT DOMAIN 341..417
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT ACT_SITE 201
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-1"
FT BINDING 4..11
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
FT BINDING 101
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OGD87664.1"
SQ SEQUENCE 420 AA; 45304 MW; B80612F9F2DCAA20 CRC64;
VGLLGAGTIG SEVFNQITLR EKELRDSFPD AAFEVKKVLV RDPLKNRRVS IPQELLTTQL
DVVVDDSSVD IIVSLLGIAD VEYEAILKAL MAGKKVVTAN KDVIARNGQE LLQTAVNKNS
ALYFEAAVAG GIQVVDNLTG RYGLNHFYAI SAILNATSNY VLSRMTSAGA ESEQALLEAQ
EKGYAEPNSE NDLNGKDAAY KIAILVSLAF REGWVNPDNI FTKGIDSLEL SDFEYALEMG
YVIKLIADAQ RTEGSLDVWV SPTLVHKNHP LASVNGVTNG ILLSGNPIGQ IKLEGLGAGS
EPTSASVLSD IMRAAQDGTP LNINLDSAQV MEPGESVGRN YIRMTVLDRP GVTAEITKII
GDNRINIDEI RQLESATDGT LANTVFLTGF SGQGSLHRAI REISDLDVCQ KINSVMRVMR
//
