ID A2T0A6_9BACT Unreviewed; 195 AA.
AC A2T0A6;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 2.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213};
DE EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213};
DE Flags: Fragment;
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:ABD33955.2};
RN [1] {ECO:0000313|EMBL:ABD33955.2}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16762628; DOI=10.1053/j.gastro.2006.02.055;
RA Konrad A., Cong Y., Duck L.W., Borlazza R., Elson C.O.;
RT "Tight mucosal compartmentation of the murine immune response to antigens
RT of the enteric microbiota.";
RL Gastroenterology 130:2050-2059(2006).
RN [2] {ECO:0000313|EMBL:ABD33955.2}
RP NUCLEOTIDE SEQUENCE.
RA Quirk P.G., Krulwich T.A.;
RL Submitted (JUL-2018) 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; DQ380420; ABD33955.2; -; Genomic_DNA.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00465.
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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
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; PF00742; Homoserine_dh; 1.
DR Pfam; PF03447; NAD_binding_3; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 5..94
FT /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF03447"
FT DOMAIN 102..155
FT /note="Homoserine dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00742"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABD33955.2"
FT NON_TER 195
FT /evidence="ECO:0000313|EMBL:ABD33955.2"
SQ SEQUENCE 195 AA; 21245 MW; 3FA6B22F629DA7F6 CRC64;
KLGEPLQVKA VLVRHFKDGP YRQLMTDDFK KIEEDGGIRV VVETIGGVEA AYEYTKRCLS
AGKHVVTANK QLVAEKGCEL LALAKKKNVS YLFEASVGGG IPVLHPLTQC MAANRIDEVY
GILNGTTNYI LTRMVRTGAF FSDALREAXA KGYARGGPHR RRGGHXRGAE NLAFWGIWPF
GSKSACXLXT PGSTC
//