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Entry: A0A0D6WUX9_9ACTN
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ID   A0A0D6WUX9_9ACTN        Unreviewed;       160 AA.
AC   A0A0D6WUX9;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   08-MAY-2019, entry version 20.
DE   RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase {ECO:0000256|SAAS:SAAS01082258};
DE            EC=1.17.1.8 {ECO:0000256|SAAS:SAAS01081445};
DE   Flags: Fragment;
GN   ORFNames=SF23_04245 {ECO:0000313|EMBL:KIX78850.1};
OS   Streptomyces sp. MBRL 10.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1592727 {ECO:0000313|EMBL:KIX78850.1};
RN   [1] {ECO:0000313|EMBL:KIX78850.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBRL 10 {ECO:0000313|EMBL:KIX78850.1};
RA   Ningthoujam D.S., Khunjanmayum R., Tamreihao K., Mande S.C.,
RA   Kumar C.M.S.;
RT   "Whole genome sequence of Streptomyces sp. strain MBRL 10, an
RT   actinobacterium with promising plant growth promoting and biocontrol
RT   activities against rice fungal pathogens.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of 4-hydroxy-
CC       tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
CC       {ECO:0000256|SAAS:SAAS01081415}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) =
CC         (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH;
CC         Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:67139; EC=1.17.1.8;
CC         Evidence={ECO:0000256|SAAS:SAAS01117954};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) =
CC         (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH;
CC         Xref=Rhea:RHEA:35331, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16845, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:67139; EC=1.17.1.8;
CC         Evidence={ECO:0000256|SAAS:SAAS01117970};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
CC       {ECO:0000256|SAAS:SAAS01081412}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS01082308}.
CC   -!- SIMILARITY: Belongs to the DapB family.
CC       {ECO:0000256|SAAS:SAAS01081404}.
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:KIX78850.1}.
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DR   EMBL; JXOL01000074; KIX78850.1; -; Genomic_DNA.
DR   EnsemblBacteria; KIX78850; KIX78850; SF23_04245.
DR   PATRIC; fig|1592727.3.peg.1396; -.
DR   UniPathway; UPA00034; UER00018.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IEA:UniProtKB-EC.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR022663; DapB_C.
DR   InterPro; IPR000846; DapB_N.
DR   InterPro; IPR022664; DapB_N_CS.
DR   InterPro; IPR023940; DHDPR_bac.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR20836; PTHR20836; 1.
DR   Pfam; PF05173; DapB_C; 1.
DR   Pfam; PF01113; DapB_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS01298; DAPB; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|SAAS:SAAS01081390};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS01082282};
KW   Diaminopimelate biosynthesis {ECO:0000256|SAAS:SAAS01081418};
KW   Lysine biosynthesis {ECO:0000256|SAAS:SAAS01081406};
KW   NAD {ECO:0000256|SAAS:SAAS01081420};
KW   NADP {ECO:0000256|SAAS:SAAS00333002};
KW   Oxidoreductase {ECO:0000256|SAAS:SAAS00333034}.
FT   DOMAIN        5    108       DapB_N. {ECO:0000259|Pfam:PF01113}.
FT   DOMAIN      111    155       DapB_C. {ECO:0000259|Pfam:PF05173}.
FT   NON_TER     160    160       {ECO:0000313|EMBL:KIX78850.1}.
SQ   SEQUENCE   160 AA;  16791 MW;  82BCB9721A3A122B CRC64;
     MSKLRVAVIG ARGRIGSEAV KAVEAAEDME LVAALGRGDK LETLTEAGAQ VAVELTTPAS
     VMENLEFLVG HGIHGVVGTT GWNEDRLAQL HTWLAASPET GVLIAPNFSI GAVLTMKFAA
     QAARYFESVE VVELHHPNKV DAPSGTAART AQLIAAARPR
//
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