ID A0A381A9B9_BRAPL Unreviewed; 419 AA. AC A0A381A9B9; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 03-MAY-2023, entry version 18. 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 Name=hom {ECO:0000313|EMBL:SUW07762.1}; GN ORFNames=NCTC13046_00521 {ECO:0000313|EMBL:SUW07762.1}; OS Brachyspira pilosicoli. OC Bacteria; Spirochaetes; Brachyspirales; Brachyspiraceae; Brachyspira. OX NCBI_TaxID=52584 {ECO:0000313|EMBL:SUW07762.1, ECO:0000313|Proteomes:UP000254237}; RN [1] {ECO:0000313|EMBL:SUW07762.1, ECO:0000313|Proteomes:UP000254237} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC13046 {ECO:0000313|EMBL:SUW07762.1, RC ECO:0000313|Proteomes:UP000254237}; RG Pathogen Informatics; RA Doyle S.; RL Submitted (JUN-2018) 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|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 --------------------------------------------------------------------------- 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; UFTN01000001; SUW07762.1; -; Genomic_DNA. DR RefSeq; WP_013243025.1; NZ_VYIY01000022.1. DR AlphaFoldDB; A0A381A9B9; -. DR EnsemblBacteria; SUW07762; SUW07762; NCTC13046_00521. DR GeneID; 56438652; -. DR OMA; LMFYGPG; -. DR UniPathway; UPA00050; UER00063. DR UniPathway; UPA00051; UER00465. DR Proteomes; UP000254237; 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 13..118 FT /note="Aspartate/homoserine dehydrogenase NAD-binding" FT /evidence="ECO:0000259|Pfam:PF03447" FT DOMAIN 135..314 FT /note="Homoserine dehydrogenase catalytic" FT /evidence="ECO:0000259|Pfam:PF00742" FT ACT_SITE 203 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR000098-1" FT BINDING 12..19 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2" FT BINDING 106 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2" FT BINDING 188 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2" SQ SEQUENCE 419 AA; 46701 MW; 04B673E1A2CC4F15 CRC64; MNESKEIKIA IAGYGNVGKG TLKTIITNNK SIERRSGFKL IVKTVFSRNI KEKHDEYLDT VENKTEDLND ILNDNEIDII VEVLGGMTTA KELILKSTKP IVTANKALLA NSLEELIKDR KSDIEFEASV AGAIPIIRAM KESLTADNIE SISGILNGTC NYILTNMTKQ KIDFNVVLKE AQDKGYAEAD PTFDIDGIDT AHKICILASM AFCNIINMKD IYIRGIRNIL LDDIIFAMGL GYTVKLVADA SIDKDNNLYV YVIPSFIKDR NFLARTSYSF NAIKITSDIA GDNVFYGVGA GGINTSSAIV SDIISIAKNK AISNELFSPI LGFSNYNNDL VIKDFRDKEE DFYVRFKSLK NKIDSFVNAF NNSSINVDKT LNKDNNMMFI LRKTTINNIL NSIKTVEDIE NIFIAKIKH //