DAPA1_WHEAT
ID DAPA1_WHEAT Reviewed; 388 AA.
AC P24846;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase 1, chloroplastic;
DE Short=HTPA synthase 1;
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 63-79.
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; M60598; AAA34263.1; -; mRNA.
DR PIR; A39213; WZWTH7.
DR AlphaFoldDB; P24846; -.
DR SMR; P24846; -.
DR PRIDE; P24846; -.
DR BRENDA; 4.3.3.7; 6500.
DR UniPathway; UPA00034; UER00017.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; P24846; baseline.
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..62
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:2211639"
FT CHAIN 63..388
FT /note="4-hydroxy-tetrahydrodipicolinate synthase 1,
FT chloroplastic"
FT /id="PRO_0000007203"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 217
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 245
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250"
FT SITE 130
FT /note="Part of a proton relay during catalysis"
FT /evidence="ECO:0000250"
FT SITE 193
FT /note="Part of a proton relay during catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 388 AA; 42413 MW; 9F054AFA75BA54D0 CRC64;
MPYLQPPRPH PHPHPTSRLS RASPPSPFPF FPAGTSRSGR LQPVPVSGHS ASRVSKGKFA
VAAVTLDDYL PMRSTEVKNR TSTDGIKSLR LITAVKTPYL PDGRFDLEAY DSLINTQING
GAEGVIVGGT TGEGHLMSWD EHIMLIGHTV NCFGANIKVI GNTGSNSTRE AVHATEQGFA
VGMHAALHVN PYYGKTSTEG LISHFKEVLP MGPTIIYNVP SRTSQDIPPP VIEALSSYSN
MAGVKECVGH ERVKCYTDKG ISIWSGNDDE CHDSRWKYGA TGVISVASNL VPGLMHSLMF
EGENAALNEK LLPLMKWLFC EPNPIGLNTA LAQLGVVRPV FRLPYTPLPL EKRVEFVRIV
EAIGRENFVG QKESRVLDDD DFVLISRY
