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Database: UniProt
Entry: T0TN61_9STRE
LinkDB: T0TN61_9STRE
Original site: T0TN61_9STRE 
ID   T0TN61_9STRE            Unreviewed;       348 AA.
AC   T0TN61;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   05-JUN-2019, entry version 29.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579};
DE            EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579};
GN   ORFNames=HSISS2_178 {ECO:0000313|EMBL:EQC72446.1};
OS   Streptococcus sp. HSISS2.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1316411 {ECO:0000313|EMBL:EQC72446.1, ECO:0000313|Proteomes:UP000015938};
RN   [1] {ECO:0000313|Proteomes:UP000015938}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HSISS2 {ECO:0000313|Proteomes:UP000015938};
RX   PubMed=24386196; DOI=10.1371/journal.pone.0083418;
RA   Van den Bogert B., Boekhorst J., Herrmann R., Smid E.J.,
RA   Zoetendal E.G., Kleerebezem M.;
RT   "Comparative genomics analysis of Streptococcus isolates from the
RT   human small intestine reveals their adaptation to a highly dynamic
RT   ecosystem.";
RL   PLoS ONE 8:e83418-e83418(2013).
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:EQC72446.1}.
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DR   EMBL; ASKC01000104; EQC72446.1; -; Genomic_DNA.
DR   EnsemblBacteria; EQC72446; EQC72446; HSISS2_178.
DR   PATRIC; fig|1316411.3.peg.188; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000015938; 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; IPR002912; ACT_dom.
DR   InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR   InterPro; IPR001342; HDH_cat.
DR   InterPro; IPR019811; HDH_CS.
DR   InterPro; IPR022697; HDH_short.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00742; Homoserine_dh; 1.
DR   Pfam; PF03447; NAD_binding_3; 1.
DR   PIRSF; PIRSF036497; HDH_short; 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};
KW   Complete proteome {ECO:0000313|Proteomes:UP000015938};
KW   Isoleucine biosynthesis {ECO:0000256|RuleBase:RU000579};
KW   Methionine biosynthesis {ECO:0000256|RuleBase:RU000579};
KW   NADP {ECO:0000256|PIRSR:PIRSR036497-2, ECO:0000256|RuleBase:RU000579};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000579,
KW   ECO:0000313|EMBL:EQC72446.1};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN      271    348       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   ACT_SITE    126    126       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR036497-1}.
FT   BINDING      26     26       NADP. {ECO:0000256|PIRSR:PIRSR036497-2}.
FT   BINDING     111    111       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR036497-2}.
SQ   SEQUENCE   348 AA;  37606 MW;  604278D94EB60152 CRC64;
     MGRIEPARTF ITKALEAGKN IVSANKDLIA THGKELITLA QDKGVAFYYE AAVAGGIPIL
     RTLANSLTSD KVTRILGVLN GTSNFMMTKM VDEGWSYEDA LKTAQELGYA ESDPTNDVEG
     IDAAYKAVIL SQFGFGATID FDDVSHKGIT NISTDDVAVA QELGYVIKLV GDVREVESGI
     SAEVSPTFLP KNHPLASVND VMNAVFVESI GIGESMYYGP GAGQKPTATS VLADIIRIAR
     RLSDGNVGKP FNEFRRDLPL ANPADVKSNY YFALDTPDEK GKILHLSEIF NSEDISFEQV
     LQQKANGTTA RIVVITHAMS KTQLQAVTEK FEAAEDFTVV NTLKVLSN
//
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