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Database: UniProt
Entry: A0A011NYE3_9PROT
LinkDB: A0A011NYE3_9PROT
Original site: A0A011NYE3_9PROT 
ID   A0A011NYE3_9PROT        Unreviewed;       422 AA.
AC   A0A011NYE3;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   16-JAN-2019, entry version 18.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579};
DE            EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579};
GN   Name=hom_1 {ECO:0000313|EMBL:EXI69667.1};
GN   ORFNames=AW08_00160 {ECO:0000313|EMBL:EXI69667.1};
OS   Candidatus Accumulibacter sp. SK-12.
OC   Bacteria; Proteobacteria; Betaproteobacteria;
OC   Candidatus Accumulibacter.
OX   NCBI_TaxID=1454001 {ECO:0000313|EMBL:EXI69667.1, ECO:0000313|Proteomes:UP000020218};
RN   [1] {ECO:0000313|EMBL:EXI69667.1, ECO:0000313|Proteomes:UP000020218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK-12 {ECO:0000313|Proteomes:UP000020218};
RA   Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT   "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT   clades.";
RL   Submitted (FEB-2014) 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}.
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:EXI69667.1}.
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DR   EMBL; JFAX01000001; EXI69667.1; -; Genomic_DNA.
DR   PATRIC; fig|1454001.3.peg.343; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000020218; 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; 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; PF01842; ACT; 1.
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:UP000020218};
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:EXI69667.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000020218};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN      342    421       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   NP_BIND       7     14       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   ACT_SITE    197    197       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000098-1}.
FT   BINDING      97     97       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   BINDING     182    182       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000098-2}.
SQ   SEQUENCE   422 AA;  44036 MW;  653E7EDAFF5B47AC CRC64;
     MTTIGVAGAG SIGASLIRLL HTSPAARSLR LKTVLVRDAA RPRPELPAGT PLTACPAELT
     DDPQIDVVVE LLGGVEEPFR IVSRALSQGK AVVTANKNLL AERGPELFAL AAERRLPLGY
     EASVCAGIPI IRTLEEALRA ERITALEGIL NGTSNYLLTR MSEERAAYAQ CLADAQRLGL
     AEPDPTYDVS GQDAACKAGI LATLAFGAYV DCRRLPVTGI DGLGLEDVRQ AEVMGYRIKL
     VAAVRRAAGD RVDAEVAAVL LPLQHPLASI RMECNAVRIE SEGLGETLLA GKGAGPAPTG
     VSLLADLLDI AAGRGRIPTD GHPFLAGAAE LADRQASAAR YYLRLAVADR PGTLAQVAGC
     FASQGISLAS VLQPEVPELA GGSLVPLILT THSTDRRRLD LVLAALSAAG CGRSVVLRIG
     EH
//
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