GenomeNet

Database: UniProt
Entry: A0A229FR16_9BURK
LinkDB: A0A229FR16_9BURK
Original site: A0A229FR16_9BURK 
ID   A0A229FR16_9BURK        Unreviewed;       436 AA.
AC   A0A229FR16;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213};
DE            EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213};
GN   ORFNames=AOC33_08100 {ECO:0000313|EMBL:OXL14471.1};
OS   Polynucleobacter cosmopolitanus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Polynucleobacter.
OX   NCBI_TaxID=351345 {ECO:0000313|EMBL:OXL14471.1, ECO:0000313|Proteomes:UP000215188};
RN   [1] {ECO:0000313|EMBL:OXL14471.1, ECO:0000313|Proteomes:UP000215188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MWH-MoIso2 {ECO:0000313|EMBL:OXL14471.1,
RC   ECO:0000313|Proteomes:UP000215188};
RA   Hahn M.W.;
RT   "Reclassification of a Polynucleobacter cosmopolitanus strain isolated from
RT   tropical Lake Victoria as Polynucleobacter victoriensis comb. nov.";
RL   Submitted (JUN-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   -!- 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:OXL14471.1}.
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; NJGG01000003; OXL14471.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A229FR16; -.
DR   OrthoDB; 9808167at2; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000215188; 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: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   NADP {ECO:0000256|PIRSR:PIRSR000098-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:OXL14471.1}.
FT   DOMAIN          355..435
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   ACT_SITE        205
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         105
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
FT   BINDING         190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
SQ   SEQUENCE   436 AA;  46590 MW;  1DB2AA4CA7483D0F CRC64;
     MKPIQVGLLG IGTVGGGVFS VLDRNQEEIT RRAGRGIKIH TVADLDTKRA EELVKGRAKV
     VSDAKQVVND PEIDVVVELI GGYGIAKELV LAAINNGKHV VTANKALLAV HGNEIFAAAQ
     AKGVTVNFEA AVAGGIPIIK ALREGLTANR IEWIAGIING TTNFILSEMR DKGLDFDVVL
     KEAQRLGYAE ADPTFDIEGV DAAHKATIMS AIAFGIPVQF DKAHVEGITK LSAIDIKYAE
     QLGYRIKLLG ITKKTKDGIE LRVHPTLIPT KRLIANVEGA MNAVQVMGDA VGTTLYYGKG
     AGAEPTASAV IADLVDVARL QTADPEHRVP HLAFQPGSMV NTTIMPMGEI TTSYYLRLRV
     ADVTGVLADI TRILADNSIS IDAMLQREAG DGENQTDLIM LTHETKEKNI LAAIAKVEAL
     KTVEGSVTKI RLENLS
//
DBGET integrated database retrieval system