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Database: UniProt
Entry: A0A074M7B0_ERYLO
LinkDB: A0A074M7B0_ERYLO
Original site: A0A074M7B0_ERYLO 
ID   A0A074M7B0_ERYLO        Unreviewed;       446 AA.
AC   A0A074M7B0;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   10-APR-2019, entry version 17.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579};
DE            EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579};
GN   ORFNames=EH31_06400 {ECO:0000313|EMBL:KEO87783.1};
OS   Erythrobacter longus.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter.
OX   NCBI_TaxID=1044 {ECO:0000313|EMBL:KEO87783.1, ECO:0000313|Proteomes:UP000027647};
RN   [1] {ECO:0000313|EMBL:KEO87783.1, ECO:0000313|Proteomes:UP000027647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6997 {ECO:0000313|EMBL:KEO87783.1,
RC   ECO:0000313|Proteomes:UP000027647};
RA   Zheng Q.;
RT   "A comprehensive comparison of genomes of Erythrobacter spp.
RT   strains.";
RL   Submitted (APR-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:KEO87783.1}.
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DR   EMBL; JMIW01000010; KEO87783.1; -; Genomic_DNA.
DR   STRING; 1044.EH31_06400; -.
DR   EnsemblBacteria; KEO87783; KEO87783; EH31_06400.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000027647; 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:UP000027647};
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   Reference proteome {ECO:0000313|Proteomes:UP000027647};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN      367    444       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   NP_BIND      22     29       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   ACT_SITE    219    219       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000098-1}.
FT   BINDING     119    119       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   BINDING     204    204       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000098-2}.
SQ   SEQUENCE   446 AA;  45721 MW;  D3BD96B57A0498FC CRC64;
     MQTTTNWSAL LGNTSPLRIG IAGLGTVGAG VIRLLETNRE LIAARAGRAI EVTAVSARER
     GKDRGVDISG FAWEDDMTAL GSRQDVDVVV ELVGGSDGPA LTLSRAAFAG GKGLVTANKA
     MVAHHGLELA KAAEAGGLAL KFEAAVAGGI PVVKGLREGT SANQLTKVYG ILNGTCNYIL
     TTMEATGADF AETLVEAQAL GYAEADPTFD IEGVDAAHKL AILATIGFGV ELDFANVVTT
     GIVAVRAADI AQADALGFVI RLIAEADVQQ DADGPKLLQR VRPCLVAKNH PLAPVDGPTN
     AVVAEGNFSG RLLFQGPGAG DGPTASAVVA DIIDIARGDV GAPFSMPIAQ LASLGPAQPG
     GRMERTYLRF TVNDRPGVLA EITAAMRDAN VSIESLIQKG RGGDDGEVLV AMVTHEGPEA
     NVARAVELLD GSDSLTGEPL VLPIIA
//
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