ID J3EWV6_9EURY Unreviewed; 315 AA.
AC J3EWV6;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213};
DE EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213};
GN ORFNames=HSB1_16200 {ECO:0000313|EMBL:EJN59462.1};
OS Halogranum salarium B-1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae.
OX NCBI_TaxID=1210908 {ECO:0000313|EMBL:EJN59462.1, ECO:0000313|Proteomes:UP000007813};
RN [1] {ECO:0000313|EMBL:EJN59462.1, ECO:0000313|Proteomes:UP000007813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-1 {ECO:0000313|EMBL:EJN59462.1,
RC ECO:0000313|Proteomes:UP000007813};
RX PubMed=23144405; DOI=10.1128/JB.01815-12;
RA Kim K.K., Lee K.C., Lee J.S.;
RT "Draft Genome Sequence of the Extremely Halophilic Archaeon Halogranum
RT salarium B-1T.";
RL J. Bacteriol. 194:6659-6659(2012).
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:EJN59462.1}.
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DR EMBL; ALJD01000004; EJN59462.1; -; Genomic_DNA.
DR RefSeq; WP_009366698.1; NZ_ALJD01000004.1.
DR AlphaFoldDB; J3EWV6; -.
DR PATRIC; fig|1210908.3.peg.1551; -.
DR eggNOG; arCOG01351; Archaea.
DR OrthoDB; 4488at2157; -.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00465.
DR Proteomes; UP000007813; Unassembled WGS sequence.
DR GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-EC.
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; IPR006096; Glu/Leu/Phe/Val/Trp_DH_C.
DR InterPro; IPR001342; HDH_cat.
DR InterPro; IPR019811; HDH_CS.
DR InterPro; IPR022697; HDH_short.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43331; HOMOSERINE DEHYDROGENASE; 1.
DR PANTHER; PTHR43331:SF1; HOMOSERINE DEHYDROGENASE; 1.
DR Pfam; PF00208; ELFV_dehydrog; 1.
DR Pfam; PF00742; Homoserine_dh; 1.
DR PIRSF; PIRSF036497; HDH_short; 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; PS01042; HOMOSER_DHGENASE; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|PIRSR:PIRSR036497-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 4..63
FT /note="Glutamate/phenylalanine/leucine/valine/L-tryptophan
FT dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00208"
FT DOMAIN 140..311
FT /note="Homoserine dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00742"
FT ACT_SITE 207
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036497-1"
FT BINDING 9..14
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
FT BINDING 108
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
SQ SEQUENCE 315 AA; 32231 MW; 3603CDA603711ACB CRC64;
MSLRLAVLGA GAVGQSVVEL ASEYGHVVTA VADSTTATVD ADGLDPASVL DRKEREGTVG
DADIEDVLAS DYDVLVEATP TTLGDAEPGF SHVRSALEAD RHVVLANKGP VAERYDDLRS
LEADSAGTVQ FEAAVGGAIP VLSTISDFGP DHITAARGVL NGTANFILSR MAAEGLGYEH
VLAEAQDLGV AEADPSFDVE GTDAALKCVI LANVLGDGGY SLDDAEVEGI QNIPGSALDL
AAEDGRTVRL IGEATPDGVR VGPRLVPQNG TLAVSGTRNI VQLETEYAGN LNLSGRGAGG
PETATAVLSD VSRIE
//
