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Database: UniProt
Entry: A0A0C9U9H2_PAXIN
LinkDB: A0A0C9U9H2_PAXIN
Original site: A0A0C9U9H2_PAXIN 
ID   A0A0C9U9H2_PAXIN        Unreviewed;       374 AA.
AC   A0A0C9U9H2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   16-JAN-2019, entry version 14.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|PIRNR:PIRNR036497};
DE            Short=HDH {ECO:0000256|PIRNR:PIRNR036497};
DE            EC=1.1.1.3 {ECO:0000256|PIRNR:PIRNR036497};
GN   ORFNames=PAXINDRAFT_168932 {ECO:0000313|EMBL:KIJ15972.1};
OS   Paxillus involutus ATCC 200175.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Boletales; Paxilineae; Paxillaceae;
OC   Paxillus.
OX   NCBI_TaxID=664439 {ECO:0000313|EMBL:KIJ15972.1};
RN   [1] {ECO:0000313|EMBL:KIJ15972.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200175 {ECO:0000313|EMBL:KIJ15972.1};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P.,
RA   Cantor M.N., Hua S.X.;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KIJ15972.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 200175 {ECO:0000313|EMBL:KIJ15972.1};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H.,
RA   Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal
RT   Mutualists.";
RL   Submitted (FEB-2015) 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   -!- SIMILARITY: Belongs to the homoserine dehydrogenase family.
CC       {ECO:0000256|PIRNR:PIRNR036497}.
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DR   EMBL; KN819335; KIJ15972.1; -; Genomic_DNA.
DR   EnsemblFungi; KIJ15972; KIJ15972; PAXINDRAFT_168932.
DR   OrthoDB; 998704at2759; -.
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-KW.
DR   InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR   InterPro; IPR001342; HDH_cat.
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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR036497};
KW   Branched-chain amino acid biosynthesis
KW   {ECO:0000256|PIRNR:PIRNR036497};
KW   Isoleucine biosynthesis {ECO:0000256|PIRNR:PIRNR036497};
KW   Methionine biosynthesis {ECO:0000256|PIRNR:PIRNR036497};
KW   NADP {ECO:0000256|PIRNR:PIRNR036497, ECO:0000256|PIRSR:PIRSR036497-2};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR036497};
KW   Threonine biosynthesis {ECO:0000256|PIRNR:PIRNR036497}.
FT   DOMAIN       16    138       NAD_binding_3. {ECO:0000259|Pfam:
FT                                PF03447}.
FT   DOMAIN      162    371       Homoserine_dh. {ECO:0000259|Pfam:
FT                                PF00742}.
FT   NP_BIND      16     21       NADP. {ECO:0000256|PIRSR:PIRSR036497-2}.
FT   ACT_SITE    234    234       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR036497-1}.
FT   BINDING      99     99       NADP. {ECO:0000256|PIRSR:PIRSR036497-2}.
FT   BINDING     123    123       NADP. {ECO:0000256|PIRSR:PIRSR036497-2}.
FT   BINDING     219    219       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR036497-2}.
SQ   SEQUENCE   374 AA;  40177 MW;  A0C14D5BC8F318D6 CRC64;
     MSKLGPEKAI HVAVVGLGGV GKALMEQLIE TPYPINIAAI SNSRKMLLFT DGTTCFNHLQ
     WATALDAADA PDTNLDVLRD ALGALAKRST TKVVLVDNTS SEAVANAYPK FLDAGIHVVT
     PNKKAFSGDL GLYKRLIGES GSPTELPRGV FYNESTVGAG LPIISTLKDL VNTGDKVKKI
     EGVFSGTLSY IFNEYSKGQE GGPSFSSVVE IAKANGYTEP HPGDDLNGAD VARKLTILSR
     MLPGLLERLP NGHVDVQPTS LVPEALRDAN AQEFMQRLPE FDEDIARKRD EAARRGNVLR
     YVGVIEVSEG HGRVEAKLEE YPKTHAFATS LQGSDNILMF HTERYGARPL LIQGAGAGNA
     VTAMGVMSDL LKLF
//
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