ID   A0A2N3Y6K2_SACSN        Unreviewed;       297 AA.
AC   A0A2N3Y6K2;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000313|EMBL:PKW18513.1};
GN   ORFNames=A8926_6605 {ECO:0000313|EMBL:PKW18513.1};
OS   Saccharopolyspora spinosa.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharopolyspora.
OX   NCBI_TaxID=60894 {ECO:0000313|EMBL:PKW18513.1, ECO:0000313|Proteomes:UP000233786};
RN   [1] {ECO:0000313|EMBL:PKW18513.1, ECO:0000313|Proteomes:UP000233786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44228 {ECO:0000313|EMBL:PKW18513.1,
RC   ECO:0000313|Proteomes:UP000233786};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 Actinobacteria strains.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DapA family.
CC       {ECO:0000256|PIRNR:PIRNR001365}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PKW18513.1}.
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DR   EMBL; PJNB01000001; PKW18513.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N3Y6K2; -.
DR   STRING; 994479.GCA_000194155_03156; -.
DR   OrthoDB; 9778880at2; -.
DR   Proteomes; UP000233786; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   CDD; cd00408; DHDPS-like; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002220; DapA-like.
DR   InterPro; IPR020625; Schiff_base-form_aldolases_AS.
DR   InterPro; IPR020624; Schiff_base-form_aldolases_CS.
DR   PANTHER; PTHR12128:SF72; 4-HYDROXY-2-OXOGLUTARATE ALDOLASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR12128; DIHYDRODIPICOLINATE SYNTHASE; 1.
DR   Pfam; PF00701; DHDPS; 1.
DR   PIRSF; PIRSF001365; DHDPS; 1.
DR   PRINTS; PR00146; DHPICSNTHASE.
DR   SMART; SM01130; DHDPS; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS00665; DHDPS_1; 1.
DR   PROSITE; PS00666; DHDPS_2; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW   Schiff base {ECO:0000256|ARBA:ARBA00023270}.
FT   ACT_SITE        137
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   ACT_SITE        165
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   BINDING         49
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   297 AA;  31608 MW;  6A1787DFE31A6CC7 CRC64;
     MNLTLDGVLA FPATPMDNAG DRLDLNAYES LLGWITEGGV HGIIPLGSTG EFAYLDPDER
     RSIAEATVKT LSGQVPAIIG VSAVTTRDAV AYSRHAQDIG ADGILLSIPT YYALGAEQVL
     AHVQAVASST ELPLILYNNP FTSQVDLTTD LLEKLVENPT LVAVKEATMD VNRIPLIQQT
     VGDRLKVLGG GFDPYALPAF VAGARGWTTG MANLVPRLCV QLHQAAVQDR DLDRAQQLDR
     ALAPLANLLV NNNLSAAVKC GLRLIGRPAG APRPPLQPVR PEVEEQLRTA LAALDQA
//