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Database: UniProt
Entry: A0A147HAG4_9BURK
LinkDB: A0A147HAG4_9BURK
Original site: A0A147HAG4_9BURK 
ID   A0A147HAG4_9BURK        Unreviewed;       440 AA.
AC   A0A147HAG4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   16-JAN-2019, entry version 9.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579};
DE            EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579};
GN   ORFNames=NS331_03320 {ECO:0000313|EMBL:KTT26778.1};
OS   Pseudacidovorax intermedius.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Pseudacidovorax.
OX   NCBI_TaxID=433924 {ECO:0000313|EMBL:KTT26778.1, ECO:0000313|Proteomes:UP000072741};
RN   [1] {ECO:0000313|EMBL:KTT26778.1, ECO:0000313|Proteomes:UP000072741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NS331 {ECO:0000313|EMBL:KTT26778.1,
RC   ECO:0000313|Proteomes:UP000072741};
RX   PubMed=26793183;
RA   Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
RA   Patil P.B.;
RT   "Genomic Resource of Rice Seed Associated Bacteria.";
RL   Front. Microbiol. 6:1551-1551(2016).
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:KTT26778.1}.
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DR   EMBL; LDSL01000026; KTT26778.1; -; Genomic_DNA.
DR   RefSeq; WP_058640594.1; NZ_LDSL01000026.1.
DR   EnsemblBacteria; KTT26778; KTT26778; NS331_03320.
DR   PATRIC; fig|433924.3.peg.2446; -.
DR   OrthoDB; 1464088at2; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000072741; 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:UP000072741};
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:KTT26778.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000072741};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN      355    435       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   NP_BIND       9     16       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   ACT_SITE    205    205       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000098-1}.
FT   BINDING     105    105       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   BINDING     190    190       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000098-2}.
SQ   SEQUENCE   440 AA;  46888 MW;  5BE020655511B572 CRC64;
     MKPIQVGLLG IGTVGSGTFE VLRRNQEEIR RRAGRGIEIA MVADLDTERA RRVVGDGVKV
     VGDAREVIAN PEIDIVIELI GGYGIAKALV LEAIAAGKHV VTANKALLAV HGTEIFAAAH
     QRGVMVAFEA AVAGGIPIIK ALREGLTANR IEWIAGIING TTNFILSEMR DKGLDFGTVL
     KEAQRLGYAE ADPTFDIEGV DAAHKLTLMS AIAFGVPVQF DKAYVEGITQ LAAQDIKYAE
     QLGYRIKLLG VTRRTDKGIE LRVHPTLVPA KRLLANVEGA MNAVVVHGDA VGTTLYYGKG
     AGSEPTASAV IADLVDITRL HSADVQHRVP YLAFHPQSMS DLPVLPMSEV TSSYYLRLRV
     ADQAGVLAKV TGLLATAGIS IDAVLQREAE DVGGEGSTDT DLIILTHDAR EGAVDSVIAE
     LQALPTVLAP VVRLRKEELR
//
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