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Entry: A0A0A1DIJ4_NOCSI
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ID   A0A0A1DIJ4_NOCSI        Unreviewed;       189 AA.
AC   A0A0A1DIJ4;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 2.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase {ECO:0000256|ARBA:ARBA00038983};
DE            EC=1.17.1.8 {ECO:0000256|ARBA:ARBA00038983};
GN   ORFNames=KR76_10825 {ECO:0000313|EMBL:AIY17119.2};
OS   Nocardioides simplex (Arthrobacter simplex).
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Pimelobacter.
OX   NCBI_TaxID=2045 {ECO:0000313|EMBL:AIY17119.2, ECO:0000313|Proteomes:UP000030300};
RN   [1] {ECO:0000313|EMBL:AIY17119.2, ECO:0000313|Proteomes:UP000030300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM Ac-2033D {ECO:0000313|EMBL:AIY17119.2,
RC   ECO:0000313|Proteomes:UP000030300};
RX   PubMed=25573942;
RA   Shtratnikova V.Y., Schelkunov M.I., Pekov Y.A., Fokina V.V.,
RA   Logacheva M.D., Sokolov S.L., Bragin E.Y., Ashapkin V.V., Donova M.V.;
RT   "Complete Genome Sequence of Steroid-Transforming Nocardioides simplex VKM
RT   Ac-2033D.";
RL   Genome Announc. 3:0-0(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-
CC         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|ARBA:ARBA00036290};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-
CC         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|ARBA:ARBA00036097};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4.
CC       {ECO:0000256|ARBA:ARBA00037922}.
CC   -!- SIMILARITY: Belongs to the DapB family.
CC       {ECO:0000256|ARBA:ARBA00006642}.
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DR   EMBL; CP009896; AIY17119.2; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A1DIJ4; -.
DR   STRING; 2045.KR76_10825; -.
DR   KEGG; psim:KR76_10825; -.
DR   eggNOG; COG0289; Bacteria.
DR   HOGENOM; CLU_047479_0_1_11; -.
DR   Proteomes; UP000030300; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:InterPro.
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   NCBIfam; TIGR00036; dapB; 1.
DR   PANTHER; PTHR20836:SF0; 4-HYDROXY-TETRAHYDRODIPICOLINATE REDUCTASE 1, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR20836; DIHYDRODIPICOLINATE REDUCTASE; 1.
DR   Pfam; PF05173; DapB_C; 1.
DR   Pfam; PF01113; DapB_N; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS01298; DAPB; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Diaminopimelate biosynthesis {ECO:0000256|ARBA:ARBA00022915};
KW   Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000313|EMBL:AIY17119.2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030300}.
FT   DOMAIN          1..47
FT                   /note="Dihydrodipicolinate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01113"
FT   DOMAIN          50..186
FT                   /note="Dihydrodipicolinate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05173"
SQ   SEQUENCE   189 AA;  19917 MW;  84BB28DE3291B6A8 CRC64;
     MDNLRYCIEN GIHAVVGTTG FDDARLDTLR GWLAEHPGTG VLIAPNFSIG AILMMRFSAI
     AAPFFESVEV VELHHPTKAD APSGTAGRTA EIIAAARREA GCDPMPDATS TGLEGARGAD
     VDGVRVHSVR VRGLVAHQEV ILGGLGETLT IRHDSLDRVS FTPGVLAGVR KIGDFPGLTV
     GLEHFLDLG
//
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