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Database: UniProt
Entry: A0A239SQT8_9STRE
LinkDB: A0A239SQT8_9STRE
Original site: A0A239SQT8_9STRE 
ID   A0A239SQT8_9STRE        Unreviewed;       428 AA.
AC   A0A239SQT8;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   10-APR-2019, entry version 7.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579};
DE            EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579};
GN   Name=thrA_1 {ECO:0000313|EMBL:SNU87726.1};
GN   ORFNames=SAMEA4412692_00757 {ECO:0000313|EMBL:SNU87726.1};
OS   Streptococcus merionis.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=400065 {ECO:0000313|EMBL:SNU87726.1, ECO:0000313|Proteomes:UP000215185};
RN   [1] {ECO:0000313|EMBL:SNU87726.1, ECO:0000313|Proteomes:UP000215185}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC13788 {ECO:0000313|EMBL:SNU87726.1,
RC   ECO:0000313|Proteomes:UP000215185};
RG   Pathogen Informatics;
RL   Submitted (JUN-2017) 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}.
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DR   EMBL; LT906439; SNU87726.1; -; Genomic_DNA.
DR   RefSeq; WP_018372655.1; NZ_LT906439.1.
DR   STRING; 1123308.KB904538_gene103; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000215185; Chromosome 1.
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; 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};
KW   Complete proteome {ECO:0000313|Proteomes:UP000215185};
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:SNU87726.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215185};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN      351    425       ACT. {ECO:0000259|PROSITE:PS51671}.
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;  46711 MW;  2D3C7C6B8A654C23 CRC64;
     MSVKIALLGF GTVASGVPFL LKESSEKIQQ AAKSEIEIVK VLVRDEDEKK ALLAKGHHHA
     FVTDIDDIIN DSEIAIVVEL MGRIEPAKTF ITRALESGKH VVTANKDLLA VYGSELFEIA
     NKNNVALYYE AAVAGGIPIL RTLANSFTSD KITRILGVLN GTSNFMMTKM VEEGWSYEAA
     LAKAQELGYA ESDPTNDVDG VDAAYKAVIL SQFAFGMTID FEDVIHKGIR DITPADVSLA
     QDLGYVIKLV ASIEETSSGL AAEVSPTFLP KDHPLAVVTG VMNAVFVESI GVGESMFYGP
     GAGQKPTAAS VVADIIRITR RLHDKTVGKS FNEYSRPAQL AKAEDIKSAY YFSIQTPDQP
     DQILRLMEIF EAEKIFLKQV LQRQSGKDAV RVVIVTRTLN KTQLKNVTEQ LEAVNDFKVN
     NILRVLGE
//
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