DAPA_MAIZE
ID DAPA_MAIZE Reviewed; 380 AA.
AC P26259;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase, chloroplastic;
DE Short=HTPA synthase;
DE EC=4.3.3.7;
DE Flags: Precursor;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 55-62.
RC STRAIN=cv. Black Mexican Sweet;
RX PubMed=1886613; DOI=10.1007/bf00282478;
RA Frisch D.A., Tommey A.M., Somers D.A., Gengenbach B.G.;
RT "Direct genetic selection of a maize cDNA for dihydrodipicolinate synthase
RT in an Escherichia coli dapA-auxotroph.";
RL Mol. Gen. Genet. 228:287-293(1991).
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; X52850; CAA37038.1; ALT_SEQ; mRNA.
DR PIR; S16560; WZZMP.
DR RefSeq; NP_001105425.1; NM_001111955.1.
DR AlphaFoldDB; P26259; -.
DR SMR; P26259; -.
DR STRING; 4577.GRMZM2G027835_P01; -.
DR PaxDb; P26259; -.
DR GeneID; 542379; -.
DR KEGG; zma:542379; -.
DR MaizeGDB; 60647; -.
DR eggNOG; ENOG502QQ8M; Eukaryota.
DR OrthoDB; 1238597at2759; -.
DR SABIO-RK; P26259; -.
DR UniPathway; UPA00034; UER00017.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P26259; baseline and 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..54
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:1886613"
FT CHAIN 55..380
FT /note="4-hydroxy-tetrahydrodipicolinate synthase,
FT chloroplastic"
FT /id="PRO_0000007200"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 209
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 237
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000250"
FT SITE 122
FT /note="Part of a proton relay during catalysis"
FT /evidence="ECO:0000250"
FT SITE 185
FT /note="Part of a proton relay during catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 380 AA; 41244 MW; 61D4CAB9D1835D11 CRC64;
MISPTNLLPA RKITPVSNGG AATASPSSPS VAARPRRLPS GLQSVTGRGK VSLAAITLDD
YLPMRSTEVK NRTSTDDITR LRLITAVKTP YLPDGRFDLE AYDSLINMQI EGGAEGVIVG
GTTGEGHLMS WDEHIMLIGH TVNCFGSRIK VIGNTGSNST REAVHATEQG FAVGMHAALH
INPYYGKTSA EGMISHFEAV LPMGPTIIYN VPSRSAQDIP PEVILAISGY TNMAGVKECV
GHERVKHYAD KGITIWSGND DECHDSKWKH GATGVISVTS NLVPGLMHSL MYKGENATLN
EKLSPLMKWL FCQPNPIALN TALAQLGVAR PVFRLPYVPL PLEKRAEFVR IVESIGRENF
VGQKEARVLD DDDFVLISRY
