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Entry: A0A1H8CCE1_9BACT
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ID   A0A1H8CCE1_9BACT        Unreviewed;       393 AA.
AC   A0A1H8CCE1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   16-JAN-2019, entry version 7.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|PIRNR:PIRNR036497, ECO:0000256|RuleBase:RU000579};
DE            Short=HDH {ECO:0000256|PIRNR:PIRNR036497};
DE            EC=1.1.1.3 {ECO:0000256|PIRNR:PIRNR036497, ECO:0000256|RuleBase:RU000579};
GN   ORFNames=SAMN05216436_10976 {ECO:0000313|EMBL:SEM92670.1};
OS   bacterium A37T11.
OC   Bacteria.
OX   NCBI_TaxID=1855384 {ECO:0000313|EMBL:SEM92670.1, ECO:0000313|Proteomes:UP000199094};
RN   [1] {ECO:0000313|EMBL:SEM92670.1, ECO:0000313|Proteomes:UP000199094}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A37T11 {ECO:0000313|EMBL:SEM92670.1,
RC   ECO:0000313|Proteomes:UP000199094};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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|PIRNR:PIRNR036497,
CC         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|PIRNR:PIRNR036497, ECO:0000256|RuleBase:RU004171}.
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DR   EMBL; FOBR01000009; SEM92670.1; -; Genomic_DNA.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000199094; 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; 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; PS01042; HOMOSER_DHGENASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR036497,
KW   ECO:0000256|RuleBase:RU000579};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR036497,
KW   ECO:0000256|RuleBase:RU000579};
KW   Complete proteome {ECO:0000313|Proteomes:UP000199094};
KW   Isoleucine biosynthesis {ECO:0000256|PIRNR:PIRNR036497,
KW   ECO:0000256|RuleBase:RU000579};
KW   Methionine biosynthesis {ECO:0000256|PIRNR:PIRNR036497,
KW   ECO:0000256|RuleBase:RU000579};
KW   NADP {ECO:0000256|PIRNR:PIRNR036497, ECO:0000256|PIRSR:PIRSR036497-2,
KW   ECO:0000256|RuleBase:RU000579};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR036497,
KW   ECO:0000256|RuleBase:RU000579};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199094};
KW   Threonine biosynthesis {ECO:0000256|PIRNR:PIRNR036497,
KW   ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN       11    120       NAD_binding_3. {ECO:0000259|Pfam:
FT                                PF03447}.
FT   DOMAIN      128    306       Homoserine_dh. {ECO:0000259|Pfam:
FT                                PF00742}.
FT   NP_BIND      11     16       NADP. {ECO:0000256|PIRSR:PIRSR036497-2}.
FT   ACT_SITE    196    196       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR036497-1}.
FT   BINDING      96     96       NADP. {ECO:0000256|PIRSR:PIRSR036497-2}.
FT   BINDING     181    181       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR036497-2}.
SQ   SEQUENCE   393 AA;  44297 MW;  2579691075D80667 CRC64;
     MSKKLTLGLF GFGVVGQGLY DIIKTKELNL SIKKFVIKHA EKKRSLPSEL FTTNAGAILN
     DPEINTVVEL IDDAEAAFQV VSTALKSGKN VVSANKKMIA YHLKELVNIQ QEYGTSLLYE
     GSVCGSIPII RNLEEYYDNE LLHSVTGIFN GSSNYILSKI FNEDMSYDKA LRQAQDLGFA
     ETDPTLDVGG FDPKFKLTIV ASHAYGLYLN PDEILNIGIT HLANPDIHYA REKNLKIKLV
     PTAREINDRQ VILYVLPKLI KPSNILYGVE NENNGVLVKA AFADEQFFYG KGAGGHPTGS
     AVLSDITALR YDYRYEYKKH LGAANLSYSD DWEITVYLRY EDESLIEKLG FIELLERHYA
     LDFKYVIGRI NLSKIWQHRD LINREGNFIA EFS
//
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