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Database: UniProt
Entry: A0A0E3WW47_9EURY
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Original site: A0A0E3WW47_9EURY 
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}.
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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
//
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