ID   A0A2N9VUR1_9HYPH        Unreviewed;       303 AA.
AC   A0A2N9VUR1;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   02-APR-2025, entry version 24.
DE   SubName: Full=Dihydrodipicolinate synthase family protein {ECO:0000313|EMBL:PIO43229.1};
GN   ORFNames=B5P45_19320 {ECO:0000313|EMBL:PIO43229.1};
OS   Phyllobacterium zundukense.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Phyllobacteriaceae; Phyllobacterium.
OX   NCBI_TaxID=1867719 {ECO:0000313|EMBL:PIO43229.1, ECO:0000313|Proteomes:UP000232163};
RN   [1] {ECO:0000313|Proteomes:UP000232163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tri-38 {ECO:0000313|Proteomes:UP000232163};
RA   Safronova V., Belimov A., Sazanova A., Kuznetsova I., Popova J.,
RA   Andronov E., Verkhozina A., Tikhonovich I.;
RT   "Does the Miocene-Pliocene relict legume Oxytropis triphylla form nitrogen-
RT   fixing nodules with a combination of bacterial strains?";
RL   Int J Environ Stud 74:706-714(2017).
CC   -!- SIMILARITY: Belongs to the DapA family. {ECO:0000256|ARBA:ARBA00007592,
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:PIO43229.1}.
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DR   EMBL; MZMT01000044; PIO43229.1; -; Genomic_DNA.
DR   RefSeq; WP_100003205.1; NZ_CP017943.1.
DR   AlphaFoldDB; A0A2N9VUR1; -.
DR   KEGG; pht:BLM14_26765; -.
DR   OrthoDB; 9778880at2; -.
DR   Proteomes; UP000232163; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IEA:TreeGrafter.
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   PANTHER; PTHR12128:SF66; 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.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW   Reference proteome {ECO:0000313|Proteomes:UP000232163}.
FT   ACT_SITE        134
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   ACT_SITE        162
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   BINDING         46
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT   BINDING         203
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   303 AA;  32857 MW;  4510F063C7372505 CRC64;
     MNFEGIYTPA ITPLSPDGQI DKKAFAAVLE SLIEAKIHGI IVGGSTGEYY AQTAQERFDL
     GSYAREVIGT RMPLILGTGA TRTEDSVAYA TAAKEIGADA ILVSSPPYAL PTERENAVHA
     LTIDRAANLP IMLYNYPARM GVMMGDEYFS RVGKSRNVVA IKESSGDTGN LHLLARKFPH
     ISLSCGWDDQ ALEFFAWGAK SWVCAGSNFL PREHVALYEA CVLEKNFDNG RAIMTAMLPL
     MDFLECGKFV QSIKHGCEII GLKAGGVRAP LRPLNSEEKR TLETVVATIK RTVAQITSGA
     NHA
//