ID   DAPA_TOBAC              Reviewed;         359 AA.
AC   Q42948;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic;
DE            Short=HTPA synthase;
DE            EC=4.3.3.7;
DE   Flags: Precursor;
GN   Name=DHPS1;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Verginiana;
RX   PubMed=8528284; DOI=10.1046/j.1365-313x.1995.08050733.x;
RA   Ghislain M., Frankard V., Jacobs M.;
RT   "A dinucleotide mutation in dihydrodipicolinate synthase of Nicotiana
RT   sylvestris leads to lysine overproduction.";
RL   Plant J. 8:733-743(1995).
CC   -!- FUNCTION: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde
CC       [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
CC       {ECO:0000250}.
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   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the DapA family. {ECO:0000305}.
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; X79675; CAA56123.1; -; mRNA.
DR   PIR; T03214; T03214.
DR   RefSeq; NP_001313049.1; NM_001326120.1.
DR   AlphaFoldDB; Q42948; -.
DR   SMR; Q42948; -.
DR   STRING; 4097.Q42948; -.
DR   GeneID; 107823498; -.
DR   KEGG; nta:107823498; -.
DR   PhylomeDB; Q42948; -.
DR   UniPathway; UPA00034; UER00017.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IBA:GO_Central.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
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   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   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   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; Chloroplast; Diaminopimelate biosynthesis; Lyase;
KW   Lysine biosynthesis; Plastid; Reference proteome; Schiff base;
KW   Transit peptide.
FT   TRANSIT         1..33
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..359
FT                   /note="4-hydroxy-tetrahydrodipicolinate synthase,
FT                   chloroplastic"
FT                   /id="PRO_0000007202"
FT   ACT_SITE        188
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        216
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         102
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000250"
FT   BINDING         255
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000250"
FT   SITE            101
FT                   /note="Part of a proton relay during catalysis"
FT                   /evidence="ECO:0000250"
FT   SITE            164
FT                   /note="Part of a proton relay during catalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   359 AA;  39576 MW;  D6E5408E3F67FDDE CRC64;
     MSSSIIGRCH FVADSIEAAG TKRRTTRWRS PRAAVIPSFH LPMRSNEVKN RTFADDIKAL
     RLITAIKTPY LPDGRFDLEA YDTLVNLQIE NGAEGVIVGG TTGEGQLMSW DEHIMLIGHT
     VNCFGGSIKV IGNTGSNSTR EAIHATEQGF AVGMHAALHI NPYYGKTSLE GLISHFESVL
     PMGPTIIYNV PSRTGQDIPP RVIQTMAKSP NLAGVKECVG NDRVEQYTSD GVVVWSGNDD
     ECHVSRWDYG ATGVISVTSN LVPGLMRELM FGGKNPALNS KLMPLMEWLF HEPNPIALNT
     ALAQLGVVRP VFRLPYVPLT KAKREEFVKI VKEIGRENFI GERDVQILDD NDFILVGRY