ID   DAPA_STRP2              Reviewed;         311 AA.
AC   Q04KR9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
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}; OrderedLocusNames=SPD_0901;
OS   Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=373153;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D39 / NCTC 7466;
RX   PubMed=17041037; DOI=10.1128/jb.01148-06;
RA   Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA   Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT   "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT   pneumoniae and comparison with that of unencapsulated laboratory strain
RT   R6.";
RL   J. Bacteriol. 189:38-51(2007).
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; CP000410; ABJ54534.1; -; Genomic_DNA.
DR   RefSeq; WP_000121636.1; NC_008533.2.
DR   AlphaFoldDB; Q04KR9; -.
DR   SMR; Q04KR9; -.
DR   STRING; 373153.SPD_0901; -.
DR   EnsemblBacteria; ABJ54534; ABJ54534; SPD_0901.
DR   GeneID; 60232949; -.
DR   KEGG; spd:SPD_0901; -.
DR   eggNOG; COG0329; Bacteria.
DR   HOGENOM; CLU_049343_7_1_9; -.
DR   OMA; GMDACVP; -.
DR   OrthoDB; 1438588at2; -.
DR   BioCyc; SPNE373153:G1G6V-988-MON; -.
DR   UniPathway; UPA00034; UER00017.
DR   Proteomes; UP000001452; 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   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; 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..311
FT                   /note="4-hydroxy-tetrahydrodipicolinate synthase"
FT                   /id="PRO_1000050280"
FT   ACT_SITE        140
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT   ACT_SITE        168
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT   BINDING         51
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT   BINDING         209
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT   SITE            50
FT                   /note="Part of a proton relay during catalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT   SITE            114
FT                   /note="Part of a proton relay during catalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
SQ   SEQUENCE   311 AA;  33894 MW;  225C7B53BF9102DA CRC64;
     MSYQDLKECK IITAFITPFH EDGSINFDAI PALIEHLLDH HTDGILLAGT TAESPTLTHD
     EELELFAAVQ KIVNGRVPLI AGVGTNDTRD SIEFVKEVAE FGGFAAGLAI VPYYNKPSQE
     GMYQHFKAIA DASDLPIIIY NIPGRVVVEL TPETMLRLAD HPNIIGVKEC TSLANMAYLI
     EHKPEEFLVY TGEDGDAFHA MNLGADGVIS VASHTNGDEM HEMFIAIAES DVKKAAAIQR
     KFIPKVNALF SYPSPAPVKA VLNYMGFEAG PTRLPLVPAP EEDAKRIIKV VVDGDYEATK
     ATVTGVLRPD Y