ID   DAPA2_WHEAT             Reviewed;         377 AA.
AC   P24847;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase 2, chloroplastic;
DE            Short=HTPA synthase 2;
DE            EC=4.3.3.7;
DE   Flags: Precursor;
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 52-68.
RC   STRAIN=cv. Chinese Spring;
RX   PubMed=2211639; DOI=10.1016/s0021-9258(18)38184-5;
RA   Kaneko T., Hashimoto T., Kumpaisal R., Yamada Y.;
RT   "Molecular cloning of wheat dihydrodipicolinate synthase.";
RL   J. Biol. Chem. 265:17451-17455(1990).
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   -!- ACTIVITY REGULATION: Sensitive to lysine inhibition. This inhibition
CC       increase in an allosteric manner with increasing concentration of the
CC       inhibitor.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
CC   -!- SUBUNIT: Tetramer of modified subunits derived from two genes in
CC       different combinations.
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; M60599; AAA34264.1; -; mRNA.
DR   PIR; B39213; WZWTH6.
DR   AlphaFoldDB; P24847; -.
DR   SMR; P24847; -.
DR   STRING; 4565.Traes_2DL_D0B92E21B.1; -.
DR   PRIDE; P24847; -.
DR   eggNOG; ENOG502QQ8M; Eukaryota.
DR   UniPathway; UPA00034; UER00017.
DR   Proteomes; UP000019116; Unplaced.
DR   ExpressionAtlas; P24847; differential.
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   1: Evidence at protein level;
KW   Allosteric enzyme; Amino-acid biosynthesis; Chloroplast;
KW   Diaminopimelate biosynthesis; Direct protein sequencing; Lyase;
KW   Lysine biosynthesis; Plastid; Reference proteome; Schiff base;
KW   Transit peptide.
FT   TRANSIT         1..51
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:2211639"
FT   CHAIN           52..377
FT                   /note="4-hydroxy-tetrahydrodipicolinate synthase 2,
FT                   chloroplastic"
FT                   /id="PRO_0000007204"
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;  40876 MW;  B0C08FC482BA6CDC CRC64;
     MMAAQPTANP GVRLGWKAPG ALASPPRLAL SRSAAAPLAS HRVGRGKFSA AAITTDDYLP
     MRSTEVKNRT SVDGIKSLRL ITAVKTPYLP DGRFDLEAYD SLINTQINGG AEGVIVGGTT
     GEGHLMSWDE HIMLIGHTVN CFGTNIKVIG NTGSNSTREA IHASEQGFAV GMHAALHVNP
     YYGKTSTAGL ISHFDEVLPM GPTIIYNVPS RTGQDIPPAV IEALSTYPNM AGVKECVGHE
     RVKCYTDKGI TIWSGNDDEC HDSRWKYGAT GVISVTSNLV PGLMRSLMFE GENAALNEKL
     LPLMKWLFSE PNPIGLNTAL AQLGVVRPVF RRPYAPLSLE KRTEFVRIVE AIGRENFVGQ
     KEVRVLDDDD FVLISRY