ID A0A0S7XSX7_9BACT Unreviewed; 405 AA. AC A0A0S7XSX7; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 22-FEB-2023, entry version 23. DE RecName: Full=Homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013376, ECO:0000256|RuleBase:RU000579}; DE EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213, ECO:0000256|RuleBase:RU000579}; GN ORFNames=AMJ44_10540 {ECO:0000313|EMBL:KPJ65331.1}; OS candidate division WOR-1 bacterium DG_54_3. OC Bacteria; Candidatus Saganbacteria. OX NCBI_TaxID=1703775 {ECO:0000313|EMBL:KPJ65331.1, ECO:0000313|Proteomes:UP000051861}; RN [1] {ECO:0000313|EMBL:KPJ65331.1, ECO:0000313|Proteomes:UP000051861} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DG_54_3 {ECO:0000313|EMBL:KPJ65331.1}; RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6; RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.; RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling RT among widespread estuary sediment bacteria."; RL Microbiome 3:14-14(2015). 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|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:KPJ65331.1}. 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; LIZX01000124; KPJ65331.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0S7XSX7; -. DR PATRIC; fig|1703775.3.peg.930; -. DR UniPathway; UPA00050; UER00063. DR UniPathway; UPA00051; UER00465. DR Proteomes; UP000051861; 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 CDD; cd04881; ACT_HSDH-Hom; 1. DR Gene3D; 3.30.70.260; -; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR045865; ACT-like_dom_sf. DR InterPro; IPR002912; ACT_dom. 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; PF01842; ACT; 1. DR Pfam; PF00742; Homoserine_dh; 1. DR Pfam; PF03447; NAD_binding_3; 1. DR PIRSF; PIRSF000098; Homoser_dehydrog; 1. DR SUPFAM; SSF55021; ACT-like; 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; PS51671; ACT; 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|ARBA:ARBA00022624, KW ECO:0000256|RuleBase:RU000579}; KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167, KW 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|ARBA:ARBA00022697, KW ECO:0000256|RuleBase:RU000579}. FT DOMAIN 329..403 FT /note="ACT" FT /evidence="ECO:0000259|PROSITE:PS51671" FT ACT_SITE 190 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR000098-1" FT BINDING 9..16 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2" FT BINDING 90 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2" FT BINDING 175 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2" SQ SEQUENCE 405 AA; 43643 MW; 703586D42715E53A CRC64; MGKIKIGILG LGVVGSAVAR NVKYVPEIEI VRGCDIRRVR VPCKLTRDPY KIINDPEIAI VVEAIGGINP AKKYVLAAIR SGKHVVTSNK ELVALHLDEL MTMAKKKGVS LLFEGSVGGG IPILSTLRDS LSANKIAEIY GIVNGTTNYI LSKMSEEGMA FSEALKKARE KGFAEADPRS DVEGYDAFYK AAILASVAFR AKVRAADVYR EGIEKITAED ILYAGEIGYV IKLLAIAKMI EGKLDVRVHP ALVSKQHPLA AVSENYNAIY VKGDPVGELM FYGQGAGGGP TASAIVSDIV QVSKGGGGKP ARLRRIKTRK IEDIESRYYI RLQAPDRFGV LAGISKAFAR KKVSIAAVVQ KETVGNVATI VILLHSVAEK NLKAALKIIE KLPVVRKVSN VIRIV //