ID   DAPA_CAMJD              Reviewed;         298 AA.
AC   A7H443;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000255|HAMAP-Rule:MF_00418};
DE            Short=HTPA synthase {ECO:0000255|HAMAP-Rule:MF_00418};
DE            EC=4.3.3.7 {ECO:0000255|HAMAP-Rule:MF_00418};
GN   Name=dapA {ECO:0000255|HAMAP-Rule:MF_00418};
GN   OrderedLocusNames=JJD26997_1204;
OS   Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 /
OS   269.97).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1458 / RM4099 / 269.97;
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT   "Complete genome sequence of Campylobacter jejuni subsp doylei 269.97
RT   isolated from human blood.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde
CC       [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
CC       {ECO:0000255|HAMAP-Rule:MF_00418}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-
CC         2,3,4,5-tetrahydrodipicolinate + H(+) + H2O; Xref=Rhea:RHEA:34171,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:67139, ChEBI:CHEBI:537519; EC=4.3.3.7;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00418};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
CC       {ECO:0000255|HAMAP-Rule:MF_00418}.
CC   -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000255|HAMAP-
CC       Rule:MF_00418}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00418}.
CC   -!- SIMILARITY: Belongs to the DapA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00418}.
CC   -!- CAUTION: Was originally thought to be a dihydrodipicolinate synthase
CC       (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde
CC       [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was
CC       shown in E.coli that the product of the enzymatic reaction is not
CC       dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-
CC       dipicolinic acid (HTPA), and that the consecutive dehydration reaction
CC       leading to DHDP is not spontaneous but catalyzed by DapB.
CC       {ECO:0000305}.
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DR   EMBL; CP000768; ABS44238.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7H443; -.
DR   SMR; A7H443; -.
DR   EnsemblBacteria; ABS44238; ABS44238; JJD26997_1204.
DR   KEGG; cjd:JJD26997_1204; -.
DR   HOGENOM; CLU_049343_7_0_7; -.
DR   OMA; GMDACVP; -.
DR   UniPathway; UPA00034; UER00017.
DR   Proteomes; UP000002302; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR   CDD; cd00950; DHDPS; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00418; DapA; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005263; DapA.
DR   InterPro; IPR002220; DapA-like.
DR   InterPro; IPR020625; Schiff_base-form_aldolases_AS.
DR   InterPro; IPR020624; Schiff_base-form_aldolases_CS.
DR   PANTHER; PTHR12128; PTHR12128; 1.
DR   Pfam; PF00701; DHDPS; 1.
DR   PIRSF; PIRSF001365; DHDPS; 1.
DR   PRINTS; PR00146; DHPICSNTHASE.
DR   SMART; SM01130; DHDPS; 1.
DR   TIGRFAMs; TIGR00674; dapA; 1.
DR   PROSITE; PS00665; DHDPS_1; 1.
DR   PROSITE; PS00666; DHDPS_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Diaminopimelate biosynthesis; Lyase;
KW   Lysine biosynthesis; Schiff base.
FT   CHAIN           1..298
FT                   /note="4-hydroxy-tetrahydrodipicolinate synthase"
FT                   /id="PRO_1000124019"
FT   ACT_SITE        137
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT   ACT_SITE        166
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT   BINDING         48
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT   BINDING         207
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT   SITE            47
FT                   /note="Part of a proton relay during catalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT   SITE            111
FT                   /note="Part of a proton relay during catalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
SQ   SEQUENCE   298 AA;  32701 MW;  89777DD2A62D175F CRC64;
     MDKNIIIGAM TALITPFKNG KVDEQSYARL IKRQIENGID AVVPAGTTGE SATLTHEEHR
     TCIEIAVEIC KGTKVKVLAG AGSNATHEAV DLAKFAKEHG ADGILSVAPY YNKPTQQGLY
     EHYKAIAQSV DTPVLLYNVP GRTGCEISTD TIIKLFRDCE NIYGVKEASG NIDKCVDLLA
     HEPRMMLISG EDAINYPILS NGGKGVISVT SNLLPDMISA LTHFALDENY KEAKKINDEL
     YNINKILFCE SNPIPIKTAM YIAGLIESLE FRLPLCSPSK ENFAKIEEVM KKYKIKGF