ID   A0A0J5TG20_9RHOB        Unreviewed;       292 AA.
AC   A0A0J5TG20;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Dihydrodipicolinate synthase/N-acetylneuraminate lyase {ECO:0000313|EMBL:KMK69077.1};
DE            EC=4.3.3.7 {ECO:0000313|EMBL:KMK69077.1};
GN   ORFNames=IMCC21224_113965 {ECO:0000313|EMBL:KMK69077.1};
OS   Puniceibacterium sp. IMCC21224.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Puniceibacterium.
OX   NCBI_TaxID=1618204 {ECO:0000313|EMBL:KMK69077.1, ECO:0000313|Proteomes:UP000036046};
RN   [1] {ECO:0000313|EMBL:KMK69077.1, ECO:0000313|Proteomes:UP000036046}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC21224 {ECO:0000313|EMBL:KMK69077.1,
RC   ECO:0000313|Proteomes:UP000036046};
RA   Cho J.-C., Yang S.-J., Kang I.;
RT   "Complete genome sequence of IMCC21224 belonging to the
RT   Alphaproteobacteria.";
RL   Submitted (MAY-2015) 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:KMK69077.1}.
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DR   EMBL; LDPY01000001; KMK69077.1; -; Genomic_DNA.
DR   RefSeq; WP_047996734.1; NZ_LDPY01000001.1.
DR   AlphaFoldDB; A0A0J5TG20; -.
DR   STRING; 1618204.IMCC21224_113965; -.
DR   PATRIC; fig|1618204.4.peg.4069; -.
DR   OrthoDB; 199953at2; -.
DR   Proteomes; UP000036046; 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:UP000036046}.
FT   ACT_SITE        135
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   ACT_SITE        163
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   BINDING         47
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT   BINDING         205
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   292 AA;  31367 MW;  52EA4AF86B11697C CRC64;
     MPQFEGVFPY IVSPVNGDGT VRRDVLATLC DDLIGKGVHG LAALGSTGEF AYLDAAQRAD
     VVRTTVKAAK GRVPVIAGVS STSTADAVSQ ATTYEGLGAD GIIAVIDAYF PLTESDVEGY
     FRAIADAVDL PIVIYTNPNF QRIDLSLDLI ARLATHERIN YIKDASSNTG RLLSILTRTK
     GQIDVFAASS HIPTAVMMIG GRGWMAGPAC LVPEQCVQLY RLCVAGEWDQ ALMIQKKLWA
     LNEVFNRFNL AACVKAGLSL QGYDIGDPIP PQAPLPDSQR RVLKNLLDDL SI
//