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Database: UniProt
Entry: Q8Y4A4_LISMO
LinkDB: Q8Y4A4_LISMO
Original site: Q8Y4A4_LISMO 
ID   Q8Y4A4_LISMO            Unreviewed;       428 AA.
AC   Q8Y4A4;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   08-MAY-2019, entry version 106.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579};
DE            EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579};
GN   Name=hom {ECO:0000313|EMBL:CAD00625.1};
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963 {ECO:0000313|EMBL:CAD00625.1, ECO:0000313|Proteomes:UP000000817};
RN   [1] {ECO:0000313|EMBL:CAD00625.1, ECO:0000313|Proteomes:UP000000817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e {ECO:0000313|Proteomes:UP000000817};
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A.,
RA   Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T.,
RA   Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P.,
RA   Domann E., Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O.,
RA   Entian K.D., Fsihi H., Portillo F.G., Garrido P., Gautier L.,
RA   Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.M.,
RA   Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E.,
RA   Maitournam A., Vicente J.M., Ng E., Nedjari H., Nordsiek G.,
RA   Novella S., de Pablos B., Perez-Diaz J.C., Purcell R., Remmel B.,
RA   Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.A.,
RA   Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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; AL591983; CAD00625.1; -; Genomic_DNA.
DR   PIR; AC1393; AC1393.
DR   RefSeq; NP_466070.1; NC_003210.1.
DR   RefSeq; WP_009924346.1; NC_003210.1.
DR   STRING; 169963.lmo2547; -.
DR   PaxDb; Q8Y4A4; -.
DR   EnsemblBacteria; CAD00625; CAD00625; CAD00625.
DR   GeneID; 987269; -.
DR   KEGG; lmo:lmo2547; -.
DR   PATRIC; fig|169963.11.peg.2609; -.
DR   eggNOG; ENOG4105D6E; Bacteria.
DR   eggNOG; COG0460; LUCA.
DR   HOGENOM; HOG000076615; -.
DR   KO; K00003; -.
DR   OMA; FEASVCG; -.
DR   PhylomeDB; Q8Y4A4; -.
DR   BioCyc; LMON169963:LMO2547-MONOMER; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000000817; Chromosome.
DR   GO; GO:0004412; F:homoserine dehydrogenase activity; IBA:GO_Central.
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; IBA:GO_Central.
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   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; PS51671; ACT; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000817};
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   Reference proteome {ECO:0000313|Proteomes:UP000000817};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN      351    428       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   NP_BIND      10     17       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   COILED      167    187       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    206    206       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000098-1}.
FT   BINDING     106    106       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   BINDING     191    191       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000098-2}.
SQ   SEQUENCE   428 AA;  46342 MW;  633FD3835CC48AA4 CRC64;
     MEAKLQVGVL GFGTVGSGVI HILEEHQEKI SQVTGYNISV KKVLVRDLEK NRRYETKGFE
     LTTNPSDVLD DPEIAVVVEV MGSITTAREY ILQALKAGKH VVTANKDLIA LHGDELVAVA
     QANNCDLFYE ASVAGGIPIL RTIVNSLAAD KIQKVMGIVN GTTNFMLTKM TTEKKSYEDV
     LAEAQALGFA ESDPTNDVDG IDAARKMVIM TRLAFGMNVN LDNVETNGIR GISPEDIEVA
     YQLGYKIKLV GTAEETNGTV NVNVGPVLLP KAHPLAGVNY ENNAVFVTGA AVGETMFYGP
     GAGELPTATS VVSDLITVAK NSRLGTNGNA FNSYKHETKH TPKEQVFSKY YLRLTMDDKT
     GTFLKLTQIF AEAGVGFDKI LQQPYDDFTA TVVIVTHSTS QAQLEQAIAR VKDEPEMQML
     AKYSVVEG
//
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