ID   DAPA_LIMF3              Reviewed;         311 AA.
AC   B2GC11;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   02-SEP-2026, entry version 96.
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=LAF_0857;
OS   Limosilactobacillus fermentum (strain NBRC 3956 / LMG 18251) (Lactobacillus
OS   fermentum).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=334390;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 3956 / LMG 18251;
RX   PubMed=18487258; DOI=10.1093/dnares/dsn009;
RA   Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T.,
RA   Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T.,
RA   Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T.,
RA   Hattori M.;
RT   "Comparative genome analysis of Lactobacillus reuteri and Lactobacillus
RT   fermentum reveal a genomic island for reuterin and cobalamin production.";
RL   DNA Res. 15:151-161(2008).
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-
CC         hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O + H(+);
CC         Xref=Rhea:RHEA:34171, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, 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; AP008937; BAG27193.1; -; Genomic_DNA.
DR   RefSeq; WP_012391182.1; NC_010610.1.
DR   AlphaFoldDB; B2GC11; -.
DR   SMR; B2GC11; -.
DR   KEGG; lfe:LAF_0857; -.
DR   PATRIC; fig|334390.5.peg.943; -.
DR   eggNOG; COG0329; Bacteria.
DR   HOGENOM; CLU_049343_7_1_9; -.
DR   UniPathway; UPA00034; UER00017.
DR   Proteomes; UP000001697; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd00950; DHDPS; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 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   NCBIfam; TIGR00674; dapA; 1.
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.
DR   PROSITE; PS00666; DHDPS_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Diaminopimelate biosynthesis; Lyase;
KW   Lysine biosynthesis; Reference proteome; Schiff base.
FT   CHAIN           1..311
FT                   /note="4-hydroxy-tetrahydrodipicolinate synthase"
FT                   /id="PRO_1000124045"
FT   ACT_SITE        138
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         49
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            48
FT                   /note="Part of a proton relay during catalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT   SITE            112
FT                   /note="Part of a proton relay during catalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
SQ   SEQUENCE   311 AA;  33017 MW;  2FA561A9F61E6423 CRC64;
     MTELTNADLL TAIVTPFTDE GTIDYPALDQ LTEHLLQAGN NGFVVGGTTG ETPTLSHDEK
     IELYTHFGRL IAGRVPVIAG TGSNNTAETI AFTNEVAQIE GIDYALVVVP PYNKPNQRGM
     LAHFTAVADA VELPLIIYNI PGRTGVKMET STVLTLAEHP NIAGIKQCAS LEEFQTLVEN
     RPAGFAVYTG EDAQALTTKV LGGDGVISVA AHNYAPQMRA MYDALSAGNY QVAAKLQRWL
     TPRMAALFMF PSPSPVKAVL AAQGLATDHC RLPICDLTAE EKEQLATALG LPSDALAGQL
     PTDLGEGLTN D
//