ID A0A0E3WW47_9EURY Unreviewed; 332 AA.
AC A0A0E3WW47;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213};
DE EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213};
GN ORFNames=MSHOH_2567 {ECO:0000313|EMBL:AKB79050.1};
OS Methanosarcina horonobensis HB-1 = JCM 15518.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=1434110 {ECO:0000313|EMBL:AKB79050.1, ECO:0000313|Proteomes:UP000033101};
RN [1] {ECO:0000313|EMBL:AKB79050.1, ECO:0000313|Proteomes:UP000033101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HB-1 {ECO:0000313|EMBL:AKB79050.1,
RC ECO:0000313|Proteomes:UP000033101};
RA Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT "Methanogenic archaea and the global carbon cycle.";
RL Submitted (JUL-2014) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP009516; AKB79050.1; -; Genomic_DNA.
DR RefSeq; WP_048140428.1; NZ_CP009516.1.
DR AlphaFoldDB; A0A0E3WW47; -.
DR STRING; 1434110.MSHOH_2567; -.
DR GeneID; 24831858; -.
DR KEGG; mhor:MSHOH_2567; -.
DR PATRIC; fig|1434110.4.peg.3299; -.
DR HOGENOM; CLU_009116_1_2_2; -.
DR OrthoDB; 4488at2157; -.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00465.
DR Proteomes; UP000033101; Chromosome.
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; 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; PF00742; Homoserine_dh; 1.
DR Pfam; PF03447; NAD_binding_3; 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.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|PIRSR:PIRSR036497-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AKB79050.1}.
FT DOMAIN 10..145
FT /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF03447"
FT DOMAIN 153..326
FT /note="Homoserine dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00742"
FT ACT_SITE 221
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036497-1"
FT BINDING 10..15
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
FT BINDING 121
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
SQ SEQUENCE 332 AA; 35389 MW; 8E42574FA5E04A11 CRC64;
MKTVRCSILG FGAIGQGVAE VLLMKKEYLE SIGLEILVVA IVDSRGATVN PEGVDLADCL
ARKRMKGTVA IEKFTGVEVI KSVDHELVIE TTPTNIVTGG AGLQNMLAAF ETGKDVITSN
KGPLTLKYRE LMEAAKAAGS SFRFEATVGG SMPVINLANE VLAGNRLKSI KGILNGTCNY
ILTRMLEERA SYKDILAESM ELGIAETDPT YDVDGIDTAC KLVILANAIF GLDVTYRDVE
VTGITKITPE ALEMAYERGH VIKLIGEVSR ERIHVAPRLV PINHPLDVRG TLNVASIDTE
LAGEITVTGK GAGPIETASA ILSDLIAVYG SQ
//