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Database: UniProt
Entry: L0HHG8_METFS
LinkDB: L0HHG8_METFS
Original site: L0HHG8_METFS 
ID   L0HHG8_METFS            Unreviewed;       328 AA.
AC   L0HHG8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213};
DE            EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213};
DE   Flags: Precursor;
GN   OrderedLocusNames=Metfor_1501 {ECO:0000313|EMBL:AGB02534.1};
OS   Methanoregula formicica (strain DSM 22288 / NBRC 105244 / SMSP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX   NCBI_TaxID=593750 {ECO:0000313|EMBL:AGB02534.1, ECO:0000313|Proteomes:UP000010824};
RN   [1] {ECO:0000313|Proteomes:UP000010824}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22288 / NBRC 105244 / SMSP
RC   {ECO:0000313|Proteomes:UP000010824};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Imachi H.,
RA   Tamaki H., Sekiguchi Y., Kamagata Y., Cadillo-Quiroz H., Zinder S.,
RA   Liu W.-T., Woyke T.;
RT   "Complete sequence of Methanoregula formicicum SMSP.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AGB02534.1, ECO:0000313|Proteomes:UP000010824}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22288 / NBRC 105244 / SMSP
RC   {ECO:0000313|Proteomes:UP000010824};
RX   PubMed=25189582;
RA   Yamamoto K., Tamaki H., Cadillo-Quiroz H., Imachi H., Kyrpides N.,
RA   Woyke T., Goodwin L., Zinder S.H., Kamagata Y., Liu W.T.;
RT   "Complete Genome Sequence of Methanoregula formicica SMSPT, a Mesophilic
RT   Hydrogenotrophic Methanogen Isolated from a Methanogenic Upflow Anaerobic
RT   Sludge Blanket Reactor.";
RL   Genome Announc. 2:e00870-14(2014).
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; CP003167; AGB02534.1; -; Genomic_DNA.
DR   RefSeq; WP_015285497.1; NC_019943.1.
DR   AlphaFoldDB; L0HHG8; -.
DR   STRING; 593750.Metfor_1501; -.
DR   GeneID; 14307890; -.
DR   KEGG; mfo:Metfor_1501; -.
DR   eggNOG; arCOG01351; Archaea.
DR   HOGENOM; CLU_009116_1_2_2; -.
DR   InParanoid; L0HHG8; -.
DR   OMA; LMFYGPG; -.
DR   OrthoDB; 4488at2157; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000010824; 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; 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; 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.
DR   PROSITE; PS01042; HOMOSER_DHGENASE; 1.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|PIRSR:PIRSR036497-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010824}.
FT   DOMAIN          7..135
FT                   /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03447"
FT   DOMAIN          143..318
FT                   /note="Homoserine dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00742"
FT   ACT_SITE        211
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036497-1"
FT   BINDING         7..12
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
FT   BINDING         111
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
FT   BINDING         196
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036497-2"
SQ   SEQUENCE   328 AA;  34745 MW;  8FE26856FF970AE3 CRC64;
     MKVALIGLGS VGRGAAEMIA KKDLGLTITG IADSKSGLIN NAGIDIVSVL ATKKKTGSCG
     TPGVTAADVV AKAEYDALIE VTPTNALSGE PATGYIRAAL NRKKHVVTSN KGPVALYYKE
     LKELARKNGV EFRYEATVAG AIPIMHVLEH GLAGNEILAI YGVLNGTCNF ILTRMAHEGL
     TYEQALLEAR ELGYAEADPT YDVQGIDAAI KLVILANTIW GNGVKLDAVD RTGIDLLTAD
     ALQLADEQGC TIRLIAEAIP RKNLLRVSPR ILEKNHPLVT QGTLNALTLE TDMAKEITLI
     GRGAGSVETA SAIIGDLLFI RDCHVQRP
//
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