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Database: UniProt
Entry: A0A0H2M290_VARPD
LinkDB: A0A0H2M290_VARPD
Original site: A0A0H2M290_VARPD 
ID   A0A0H2M290_VARPD        Unreviewed;       452 AA.
AC   A0A0H2M290;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   16-JAN-2019, entry version 15.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579};
DE            EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579};
GN   Name=hom1 {ECO:0000313|EMBL:KLN56524.1};
GN   ORFNames=VPARA_24660 {ECO:0000313|EMBL:KLN56524.1};
OS   Variovorax paradoxus.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=34073 {ECO:0000313|EMBL:KLN56524.1, ECO:0000313|Proteomes:UP000035170};
RN   [1] {ECO:0000313|EMBL:KLN56524.1, ECO:0000313|Proteomes:UP000035170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TBEA6 {ECO:0000313|EMBL:KLN56524.1,
RC   ECO:0000313|Proteomes:UP000035170};
RA   Poehlein A., Schuldes J., Wuebbeler J.H., Hiessl S., Steinbuechel A.,
RA   Daniel R.;
RT   "Genome sequence of Variovorax paradoxus TBEA6.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-homoserine + NADP(+) = H(+) + L-aspartate 4-
CC         semialdehyde + NADPH; Xref=Rhea:RHEA:15761, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57476, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:537519; EC=1.1.1.3;
CC         Evidence={ECO:0000256|RuleBase:RU000579};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-homoserine from L-aspartate: step 3/3.
CC       {ECO:0000256|RuleBase:RU000579}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
CC       threonine from L-aspartate: step 3/5.
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
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KLN56524.1}.
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DR   EMBL; JZWI01000011; KLN56524.1; -; Genomic_DNA.
DR   RefSeq; WP_047784727.1; NZ_JZWI01000011.1.
DR   EnsemblBacteria; KLN56524; KLN56524; VPARA_24660.
DR   PATRIC; fig|34073.19.peg.2531; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000035170; 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   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   Pfam; PF00742; Homoserine_dh; 1.
DR   Pfam; PF03447; NAD_binding_3; 1.
DR   PIRSF; PIRSF000098; Homoser_dehydrog; 1.
DR   SUPFAM; SSF51735; SSF51735; 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
KW   {ECO:0000256|RuleBase:RU000579};
KW   Complete proteome {ECO:0000313|Proteomes:UP000035170};
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|RuleBase:RU000579,
KW   ECO:0000313|EMBL:KLN56524.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035170};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN       28    147       NAD_binding_3. {ECO:0000259|Pfam:
FT                                PF03447}.
FT   DOMAIN      155    333       Homoserine_dh. {ECO:0000259|Pfam:
FT                                PF00742}.
FT   NP_BIND      27     34       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   ACT_SITE    223    223       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000098-1}.
FT   BINDING     123    123       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   BINDING     208    208       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000098-2}.
SQ   SEQUENCE   452 AA;  47064 MW;  7AA2666FE7413DBD CRC64;
     MYRDPVQSLE PLPSRPAAIR ALRVGMIGIG TVGSGTFRVL ARNQAEIAGR AGRPIELVMV
     AARNLVRAAT VVGGNVPLTD DPLRVATHPD VDVVVEVAGG TGPARDWVLA AIAHGKHVVT
     ANKALLAEHG AEIFAAARRH GVAVAYEGAV AVSIPIVKAL REGLTANRIE WVAGIINGTT
     NFILSKMRDE GLDFAAALVQ AQALGYAEAD PAFDIEGIDA AHKLTLLAAN AFGTSVRLAD
     VQVEGITALQ RVDVACAEQL GYRIKLLGVA RRSEEGVELR VQPALVPASH LMAHVNGSMN
     AVMVKGDAAG VTMYYGAGAG SEQTASAVIA DLVDVARLDG THAAQRVPHL GFHAHAMSDL
     PVLPRAAACC AHYLRIPVHA ASQIEAVSGW LAGQQVPVRQ VALAAAQPGM GAQVLVLTQP
     VRQGTMDLAL HALQAHPLVA GKVTALRVEE LA
//
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