ID A0A1Y4S9K2_9FIRM Unreviewed; 404 AA.
AC A0A1Y4S9K2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213, ECO:0000256|RuleBase:RU000579};
DE EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213, ECO:0000256|RuleBase:RU000579};
GN ORFNames=B5E77_08725 {ECO:0000313|EMBL:OUQ26567.1};
OS Lachnoclostridium sp. An131.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1965555 {ECO:0000313|EMBL:OUQ26567.1, ECO:0000313|Proteomes:UP000199743};
RN [1] {ECO:0000313|Proteomes:UP000199743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An131 {ECO:0000313|Proteomes:UP000199743};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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 -!- CATALYTIC ACTIVITY:
CC Reaction=L-homoserine + NADP(+) = H(+) + L-aspartate 4-semialdehyde +
CC NADPH; Xref=Rhea:RHEA:15761, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.1.1.3;
CC Evidence={ECO:0000256|RuleBase:RU000579};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 3/3.
CC {ECO:0000256|RuleBase:RU000579}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 3/5. {ECO:0000256|RuleBase:RU000579}.
CC -!- SIMILARITY: Belongs to the homoserine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00006753, ECO:0000256|RuleBase:RU004171}.
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:OUQ26567.1}.
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DR EMBL; NFLI01000009; OUQ26567.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4S9K2; -.
DR OrthoDB; 9808167at2; -.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00465.
DR Proteomes; UP000199743; Unassembled WGS sequence.
DR GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR InterPro; IPR016204; HDH.
DR InterPro; IPR001342; HDH_cat.
DR InterPro; IPR019811; HDH_CS.
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; PIRSF000098; Homoser_dehydrog; 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 Amino-acid biosynthesis {ECO:0000256|RuleBase:RU000579};
KW Branched-chain amino acid biosynthesis {ECO:0000256|RuleBase:RU000579};
KW Isoleucine biosynthesis {ECO:0000256|RuleBase:RU000579};
KW Methionine biosynthesis {ECO:0000256|RuleBase:RU000579};
KW NADP {ECO:0000256|PIRSR:PIRSR000098-2, ECO:0000256|RuleBase:RU000579};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000579};
KW Reference proteome {ECO:0000313|Proteomes:UP000199743};
KW Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT DOMAIN 8..124
FT /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF03447"
FT DOMAIN 132..310
FT /note="Homoserine dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00742"
FT ACT_SITE 200
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-1"
FT BINDING 7..14
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
FT BINDING 100
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
SQ SEQUENCE 404 AA; 44065 MW; 74B95A5C7E3DAE82 CRC64;
MVQIAVMGYG TVGSGVVEVL NTNQASINKR AGDEINIKYV LDLRDFPGDP VESKLIHDFE
TIVNDPEIKI VVEVMGGVEP AYTFTKRCLE AGKSVCTSNK ELVARHGAEL LEIARERELN
YLFEASVGGG IPIIRPLNSS LTADEITEIT GILNGTTNYI LTKMSYGGTD FDTALKDAQA
KGYAERNPEA DVEGYDACRK IAILTSLVSG RQVDFEDIYT EGITKITAED IKYAKKMGRA
VKLLAMSKKE DGKFFAMVAP FLINEMHPLY SVNGVFNAIF AKGNVLGDVM FYGSGAGKLP
TASAVVADVV DAAKHLHRSI MTFWSTKKLE LTDISNAKRR FFVRAKGDGQ ADAIRMAELF
GPVELVNADL EGEFGFITGK LTEAEYQECA AKTDAIIHMI RVEG
//
