ID   A0A0B3SM97_9RHOB        Unreviewed;       296 AA.
AC   A0A0B3SM97;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Dihydrodipicolinate synthase {ECO:0000313|EMBL:KHQ51649.1};
DE            EC=4.3.3.7 {ECO:0000313|EMBL:KHQ51649.1};
GN   ORFNames=OA50_03812 {ECO:0000313|EMBL:KHQ51649.1};
OS   Mameliella alba.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Mameliella.
OX   NCBI_TaxID=561184 {ECO:0000313|EMBL:KHQ51649.1, ECO:0000313|Proteomes:UP000030960};
RN   [1] {ECO:0000313|EMBL:KHQ51649.1, ECO:0000313|Proteomes:UP000030960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMTAT08 {ECO:0000313|EMBL:KHQ51649.1,
RC   ECO:0000313|Proteomes:UP000030960};
RA   Gan H.Y., Muhd D.-D., Mohd Noor M.E., Yeong Y.S., Usup G.;
RT   "Genome sequence of Ponticoccus sp. strain UMTAT08 isolated from clonal
RT   culture of toxic dinoflagellate Alexandrium tamiyavanichii.";
RL   Submitted (OCT-2014) 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:KHQ51649.1}.
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DR   EMBL; JSUQ01000016; KHQ51649.1; -; Genomic_DNA.
DR   RefSeq; WP_043144461.1; NZ_QAEF01000004.1.
DR   AlphaFoldDB; A0A0B3SM97; -.
DR   PATRIC; fig|1515334.3.peg.3838; -.
DR   OrthoDB; 9782828at2; -.
DR   Proteomes; UP000030960; Unassembled WGS sequence.
DR   GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IEA:UniProtKB-EC.
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: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.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030960}.
FT   ACT_SITE        138
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   ACT_SITE        166
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   BINDING         50
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT   BINDING         208
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   296 AA;  32786 MW;  E25F42AB94E1B74F CRC64;
     MSYNVKLSGV MPALVTPFDA DNKIDFDAFG KLLTHFRESG VTGWVPNGST GEYFSQTTEE
     RRAVLQFVKD FANDDEILIA GTNAPATREV IEQTAMAKEI GYDNVLLAPP FYTRPTQEEL
     IKHYETVLAE VDVNLVLYSY PAKDGDDISF ELMDHFADNP RVIGIKESSG VLQRAIDIVS
     RYEGKIQLIS GSDDIALDFM FWGAESWICG PSNCMAKACC ELDRLYKAGD LVAAKSLMMK
     LYRAMNILES GKFVQKIKYG AELQGMPVGE CRAPLGPLTE AEKAEFKEAM APILAM
//