ID DAPA_SOYBN Reviewed; 332 AA.
AC Q42800;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic;
DE Short=HTPA synthase;
DE EC=4.3.3.7;
DE Flags: Precursor;
GN Name=DHPS1; Synonyms=DAPA;
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Century; TISSUE=Leaf;
RX PubMed=8000011; DOI=10.1007/bf00028865;
RA Silk G.W., Matthews B.F., Somers D.A., Gengenbach B.G.;
RT "Cloning and expression of the soybean DapA gene encoding
RT dihydrodipicolinate synthase.";
RL Plant Mol. Biol. 26:989-993(1994).
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; L36436; AAA73555.1; -; mRNA.
DR PIR; S50750; S50750.
DR RefSeq; NP_001238299.1; NM_001251370.1.
DR AlphaFoldDB; Q42800; -.
DR SMR; Q42800; -.
DR STRING; 3847.Q42800; -.
DR PaxDb; 3847-GLYMA18G45380-1; -.
DR GeneID; 548067; -.
DR KEGG; gmx:548067; -.
DR eggNOG; ENOG502QQ8M; Eukaryota.
DR InParanoid; Q42800; -.
DR OrthoDB; 1780992at2759; -.
DR UniPathway; UPA00034; UER00017.
DR Proteomes; UP000008827; 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; Aldolase class I; 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 NCBIfam; TIGR00674; dapA; 1.
DR PANTHER; PTHR12128:SF15; 4-HYDROXY-TETRAHYDRODIPICOLINATE SYNTHASE 1, CHLOROPLASTIC; 1.
DR PANTHER; PTHR12128; DIHYDRODIPICOLINATE SYNTHASE; 1.
DR Pfam; PF00701; DHDPS; 1.
DR PIRSF; PIRSF001365; DHDPS; 1.
DR PRINTS; PR00146; DHPICSNTHASE.
DR SMART; SM01130; DHDPS; 1.
DR SUPFAM; SSF51569; Aldolase; 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..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..332
FT /note="4-hydroxy-tetrahydrodipicolinate synthase,
FT chloroplastic"
FT /id="PRO_0000007201"
FT ACT_SITE 161
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 189
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250"
FT SITE 74
FT /note="Part of a proton relay during catalysis"
FT /evidence="ECO:0000250"
FT SITE 137
FT /note="Part of a proton relay during catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 332 AA; 36386 MW; 5C7292056BB85BB9 CRC64;
MITNSAAVKP NFHLPMRSFE LKNRTSPEDI KALRLITAIK TPYLPDGRFD LEAYDDLVNM
QIGQGAEGVI VGGTTGEGQL MSWEEHIILI AHTVNCFGGK IKVIGNTGSN STREAIHATE
QGFAVGMHAA LHINPYYGKT SLDGMVAHFR SVLSMGPTII YNVPARTGQD IPPHVIQTLA
ESVNLAGVKE CVGNDRIKQY TDDGIVVWSG NDDQCHDARW GYGATGVVSV ASNLVPGLMR
ELMFGGVNPT LNSKLLPLID WLFHMPNPIG LNTALAQLGV IRPVFRLPFV PLPVDKRIEF
ANLVKEIGRE HFVGNKVVEV LDDDDFFLVS RY
//
