ID   DAPA_COILA              Reviewed;         377 AA.
AC   Q39535;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic;
DE            Short=HTPA synthase;
DE            EC=4.3.3.7;
DE   Flags: Precursor;
GN   Name=DAPA; Synonyms=DHPS1;
OS   Coix lacryma-jobi (Job's tears).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Rottboelliinae; Coix.
OX   NCBI_TaxID=4505;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Adlay;
RX   PubMed=10608664; DOI=10.1023/a:1006367116073;
RA   Dante R.A., Cord-Neto G., Leite A., Arruda P.;
RT   "The DapA gene encoding the lysine biosynthetic enzyme dihydrodipicolinate
RT   synthase from Coix lacryma-jobi: cloning, characterization, and expression
RT   analysis.";
RL   Plant Mol. Biol. 41:551-561(1999).
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; U61730; AAB04021.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q39535; -.
DR   SMR; Q39535; -.
DR   UniPathway; UPA00034; UER00017.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IEA:UniProtKB-EC.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Chloroplast; Diaminopimelate biosynthesis; Lyase;
KW   Lysine biosynthesis; Plastid; Schiff base; Transit peptide.
FT   TRANSIT         1..51
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           52..377
FT                   /note="4-hydroxy-tetrahydrodipicolinate synthase,
FT                   chloroplastic"
FT                   /id="PRO_0000007199"
FT   REGION          21..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        206
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        234
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         120
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000250"
FT   BINDING         273
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000250"
FT   SITE            119
FT                   /note="Part of a proton relay during catalysis"
FT                   /evidence="ECO:0000250"
FT   SITE            182
FT                   /note="Part of a proton relay during catalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   377 AA;  41079 MW;  A88DE8119F614A2D CRC64;
     MISPRMTTNL LPARTISLVS NGGAATASPS SPSVAARPRR PSSGTGRGKV SAITLDDYLP
     MRSTEVKNRT STDDITSLRL ITAVKTPYLP DGRFDLEAYD SLINMQIEGG AEGVIVGGTT
     GEGHLMSWDE HIMLIGHTVN CFGSRIKVIG NTGSNSTREA VHATEQGFAV GMHAALHINP
     YYGKTSTEGM ISHFESVLPM GPTIIYNVPS RSAQDIPPEV IVAISGYINM AGVKECIGHE
     RIKHYADKGI TIWSGNDDEC HDSRWKYGAT GVISVTSNLV PGLMHSLMYK GENAVLKEKL
     LPLMKWLFCQ PNPIALNTAL AQLGVARPVF RLPYVPLPLE KRAEFVRIVE AIGRENFVGQ
     KETRVLDDDD FVLISRY