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Database: UniProt
Entry: K0HSW9_9BURK
LinkDB: K0HSW9_9BURK
Original site: K0HSW9_9BURK 
ID   K0HSW9_9BURK            Unreviewed;       467 AA.
AC   K0HSW9;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   08-MAY-2019, entry version 40.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579};
DE            EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579};
GN   ORFNames=C380_00085 {ECO:0000313|EMBL:AFU43747.1};
OS   Acidovorax sp. KKS102.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=358220 {ECO:0000313|EMBL:AFU43747.1, ECO:0000313|Proteomes:UP000006306};
RN   [1] {ECO:0000313|EMBL:AFU43747.1, ECO:0000313|Proteomes:UP000006306}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KKS102 {ECO:0000313|EMBL:AFU43747.1,
RC   ECO:0000313|Proteomes:UP000006306};
RX   PubMed=23209225; DOI=10.1128/JB.01848-12;
RA   Ohtsubo Y., Maruyama F., Mitsui H., Nagata Y., Tsuda M.;
RT   "Complete Genome Sequence of Acidovorax sp. Strain KKS102, a
RT   Polychlorinated-Biphenyl Degrader.";
RL   J. Bacteriol. 194:6970-6971(2012).
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}.
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DR   EMBL; CP003872; AFU43747.1; -; Genomic_DNA.
DR   RefSeq; WP_015011842.1; NC_018708.1.
DR   STRING; 358220.C380_00085; -.
DR   EnsemblBacteria; AFU43747; AFU43747; C380_00085.
DR   KEGG; ack:C380_00085; -.
DR   PATRIC; fig|358220.3.peg.17; -.
DR   KO; K00003; -.
DR   OrthoDB; 1464088at2; -.
DR   BioCyc; ASP358220:G1HB5-16-MONOMER; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000006306; Chromosome.
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:UP000006306};
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   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN       30    149       NAD_binding_3. {ECO:0000259|Pfam:
FT                                PF03447}.
FT   DOMAIN      157    343       Homoserine_dh. {ECO:0000259|Pfam:
FT                                PF00742}.
FT   NP_BIND      29     36       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   ACT_SITE    225    225       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000098-1}.
FT   BINDING     125    125       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   BINDING     210    210       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000098-2}.
SQ   SEQUENCE   467 AA;  48450 MW;  AD91F024B70AFEF9 CRC64;
     MYRDPVQSLE APLLPSSATA MRPLRVGMIG IGTVGAGTFR VLARNQALIA ARAGRGIKLV
     VVCARSLARA MSVVGKDVAL TNDPMQVATH PDVDVLVEAA GGTGPARDWV LAAIRAGKHV
     VTANKALLAE HGNEIFAAAR QHGVAVAYEG AVAVSIPIVK ALREGLTANR IEWVAGIING
     TTNFILSKMR DEGVGFAEAL AQAQALGYAE ADPTFDIEGM DAAHKISLLA ANAFGMPVRF
     ADAQVEGITA LQGLDVACAE QLGFRIKLLG VAKRRKEGDA EGNLEGVELR VQPALVPATH
     LLAHVNGSMN AVMVKGDASG VTMYYGAGAG AEQTASAVIA DLVDVARLDG THAAQRVPHL
     GFHPQAVDEQ LAVLPRAAVH TRHYLRVPVH SAQQIEAVGA WLAAQQVPVL QVALALDKAL
     PPGSGPQVLV LTDAVAQSTV DLAVFALAAH PAVAGPVVTL RVETLEG
//
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