ID A0A352P2U5_9FIRM Unreviewed; 404 AA. AC A0A352P2U5; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 22-FEB-2023, entry version 16. DE RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579}; DE EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579}; GN ORFNames=DC053_07820 {ECO:0000313|EMBL:HBC99278.1}; OS Lachnoclostridium sp. OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae. OX NCBI_TaxID=2028282 {ECO:0000313|EMBL:HBC99278.1, ECO:0000313|Proteomes:UP000263023}; RN [1] {ECO:0000313|EMBL:HBC99278.1, ECO:0000313|Proteomes:UP000263023} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UBA11745 {ECO:0000313|EMBL:HBC99278.1}; RX PubMed=30148503; DOI=.1038/nbt.4229; RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A., RA Chaumeil P.A., Hugenholtz P.; RT "A standardized bacterial taxonomy based on genome phylogeny substantially RT revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). 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|ARBA:ARBA00000116, CC 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|ARBA:ARBA00005062, ECO:0000256|RuleBase:RU000579}. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine CC from L-aspartate: step 3/5. {ECO:0000256|ARBA:ARBA00005056, CC ECO:0000256|RuleBase:RU000579}. CC -!- SIMILARITY: Belongs to the homoserine dehydrogenase family. CC {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:HBC99278.1}. 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; DNNH01000084; HBC99278.1; -; Genomic_DNA. DR AlphaFoldDB; A0A352P2U5; -. DR UniPathway; UPA00050; UER00063. DR UniPathway; UPA00051; UER00465. DR Proteomes; UP000263023; 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|ARBA:ARBA00022605, KW 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|ARBA:ARBA00022857, ECO:0000256|PIRSR:PIRSR000098-2}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU000579}; 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; 44446 MW; 1F2629E54473A8B7 CRC64; MRHIAVMGYG TIGSGVVEVL ERNKEIIAKR VGDEVDVKYV LDLREFPGDP AEDKIVHDFS VIEKDQSVSM VIETMGGLNP AYPFVKASLM AGKHVATSNK ALVAAYGTEL LKIAKEHNVN FFFEASVGGG IPVIRPLYTS LAGEVVEEIT GILNGTTNYI LTKMDKAGET FETALREAQE LGYAERNPEA DVDGHDTCRK IAILTAMATG HEVNYEHIYT EGITKITDVD FRYADAMGTS VKLFGSSRIQ DGTVHAFVAP VMIGKDHPLY SVNDVYNGIL VKGNMLGTSM FYGCGAGKLP TASAVVADII EALKNKDHHV EMGWDSENLT ISAMNSISFR YFVRIRGIAD KRVKEVEAVF GKVEVVELDH MDEFAVLTET MTEEDYEIKA KKLSGIRQRI RAEF //