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Database: UniProt
Entry: A0A2C6J2C2_9PROT
LinkDB: A0A2C6J2C2_9PROT
Original site: A0A2C6J2C2_9PROT 
ID   A0A2C6J2C2_9PROT        Unreviewed;       447 AA.
AC   A0A2C6J2C2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   16-JAN-2019, entry version 6.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579};
DE            EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579};
GN   ORFNames=BG621_03000 {ECO:0000313|EMBL:PHI96724.1};
OS   Parasaccharibacter apium.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Parasaccharibacter.
OX   NCBI_TaxID=1510841 {ECO:0000313|EMBL:PHI96724.1, ECO:0000313|Proteomes:UP000222233};
RN   [1] {ECO:0000313|EMBL:PHI96724.1, ECO:0000313|Proteomes:UP000222233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AS1 {ECO:0000313|EMBL:PHI96724.1,
RC   ECO:0000313|Proteomes:UP000222233};
RA   Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL   Submitted (SEP-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|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:PHI96724.1}.
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DR   EMBL; MEJG01000002; PHI96724.1; -; Genomic_DNA.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000222233; 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; 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; 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:UP000222233};
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:UP000222233};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN       23    143       NAD_binding_3. {ECO:0000259|Pfam:
FT                                PF03447}.
FT   DOMAIN      151    329       Homoserine_dh. {ECO:0000259|Pfam:
FT                                PF00742}.
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   447 AA;  47438 MW;  C6234ABEA57FE5AD CRC64;
     MTTAHRNTVS SPALPPLRLG IAGLGTVGTG VIRLLRTHMA LLQSRTGRQI EVIAVSARNR
     TRDRGIDLSA LQWYDNPIAL AAAPDIDVVV ELMGGADGAA RALVEAALKA GKAVVTANKA
     LVARHAQTLA RLSHKHDAPL LFEAAVAGGI PAIKMVREGV APDALTRLGG ILNGTSNFIL
     TEMAETGRAF DDVLKEAQEK GYAEADPSAD IDGWDAAHKL SILTAIAFRP ILFDSLAVSG
     MRRITTSDIH QARKLGYAIK MLGVARRLAD DRVEAWVQPC LIPAQSGLAQ VNGVYNALTT
     EGPFSGPITI SGQGAGEGPT ANAVMADIID LARGHTLPLW GRMAEQAPIA CEPIEDLPSR
     FYLRITLKTP SDAVPDATTA LREVRTILEN EALPVESGHH HMEGDAAQLI FLTGTTSLAE
     INRLLPILEE VAFINGTPLA LKLEDLP
//
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