ID   DAPA1_ARATH             Reviewed;         365 AA.
AC   Q9LZX6; O49355; Q8VZQ1; Q9SW58;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   21-NOV-2003, sequence version 2.
DT   27-MAR-2024, entry version 163.
DE   RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase 1, chloroplastic;
DE            Short=HTPA synthase 1;
DE            EC=4.3.3.7;
DE   Flags: Precursor;
GN   Name=DHDPS1; Synonyms=DHDPS, DHPS1; OrderedLocusNames=At3g60880;
GN   ORFNames=T4C21_290;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   PubMed=8049377; DOI=10.1007/bf00043882;
RA   Vauterin M., Jacobs M.;
RT   "Isolation of a poplar and an Arabidopsis thaliana dihydrodipicolinate
RT   synthase cDNA clone.";
RL   Plant Mol. Biol. 25:545-550(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE OF 1-159 (ISOFORM 2).
RA   Vauterin M.;
RL   Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
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-
CC         hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O;
CC         Xref=Rhea:RHEA:34171, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, 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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9LZX6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9LZX6-2; Sequence=VSP_009000;
CC   -!- MISCELLANEOUS: [Isoform 1]: May be due to a competing acceptor splice
CC       site.
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; X72971; CAB45642.1; -; mRNA.
DR   EMBL; AL162295; CAB82692.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE80120.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE80121.1; -; Genomic_DNA.
DR   EMBL; AY063943; AAL36299.1; -; mRNA.
DR   EMBL; AY096442; AAM20082.1; -; mRNA.
DR   EMBL; AY087718; AAM65255.1; -; mRNA.
DR   EMBL; X98080; CAA66703.1; -; Genomic_DNA.
DR   PIR; S46304; S46304.
DR   PIR; T47899; T47899.
DR   RefSeq; NP_191647.1; NM_115952.2. [Q9LZX6-2]
DR   RefSeq; NP_850730.1; NM_180399.3. [Q9LZX6-1]
DR   PDB; 6VVH; X-ray; 1.79 A; AAA/BBB/CCC/DDD=49-365.
DR   PDB; 6VVI; X-ray; 2.15 A; AAA/BBB/CCC/DDD=49-365.
DR   PDB; 7MDS; X-ray; 2.29 A; A/B=49-365.
DR   PDBsum; 6VVH; -.
DR   PDBsum; 6VVI; -.
DR   PDBsum; 7MDS; -.
DR   AlphaFoldDB; Q9LZX6; -.
DR   SMR; Q9LZX6; -.
DR   BioGRID; 10573; 2.
DR   STRING; 3702.Q9LZX6; -.
DR   PaxDb; 3702-AT3G60880-2; -.
DR   ProteomicsDB; 224706; -. [Q9LZX6-1]
DR   EnsemblPlants; AT3G60880.1; AT3G60880.1; AT3G60880. [Q9LZX6-2]
DR   EnsemblPlants; AT3G60880.2; AT3G60880.2; AT3G60880. [Q9LZX6-1]
DR   GeneID; 825259; -.
DR   Gramene; AT3G60880.1; AT3G60880.1; AT3G60880. [Q9LZX6-2]
DR   Gramene; AT3G60880.2; AT3G60880.2; AT3G60880. [Q9LZX6-1]
DR   KEGG; ath:AT3G60880; -.
DR   Araport; AT3G60880; -.
DR   TAIR; AT3G60880; DHDPS1.
DR   eggNOG; ENOG502QQ8M; Eukaryota.
DR   InParanoid; Q9LZX6; -.
DR   OMA; THDEHCR; -.
DR   OrthoDB; 1780992at2759; -.
DR   PhylomeDB; Q9LZX6; -.
DR   BioCyc; ARA:AT3G60880-MONOMER; -.
DR   UniPathway; UPA00034; UER00017.
DR   PRO; PR:Q9LZX6; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LZX6; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IDA:TAIR.
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   HAMAP; MF_00418; DapA; 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   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.
DR   Genevisible; Q9LZX6; AT.
PE   1: Evidence at protein level;
KW   3D-structure; Allosteric enzyme; Alternative splicing;
KW   Amino-acid biosynthesis; Chloroplast; Diaminopimelate biosynthesis; Lyase;
KW   Lysine biosynthesis; Plastid; Reference proteome; Schiff base;
KW   Transit peptide.
FT   TRANSIT         1..39
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           40..365
FT                   /note="4-hydroxy-tetrahydrodipicolinate synthase 1,
FT                   chloroplastic"
FT                   /id="PRO_0000007197"
FT   ACT_SITE        194
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        222
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000250"
FT   BINDING         261
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000250"
FT   SITE            107
FT                   /note="Part of a proton relay during catalysis"
FT                   /evidence="ECO:0000250"
FT   SITE            170
FT                   /note="Part of a proton relay during catalysis"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         30
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:8049377, ECO:0000303|Ref.5"
FT                   /id="VSP_009000"
FT   CONFLICT        286
FT                   /note="A -> E (in Ref. 1; CAB45642)"
FT                   /evidence="ECO:0000305"
FT   HELIX           60..64
FT                   /evidence="ECO:0007829|PDB:7MDS"
FT   STRAND          68..71
FT                   /evidence="ECO:0007829|PDB:7MDS"
FT   STRAND          80..82
FT                   /evidence="ECO:0007829|PDB:7MDS"
FT   HELIX           84..96
FT                   /evidence="ECO:0007829|PDB:7MDS"
FT   STRAND          101..106
FT                   /evidence="ECO:0007829|PDB:7MDS"
FT   TURN            107..110
FT                   /evidence="ECO:0007829|PDB:7MDS"
FT   HELIX           111..113
FT                   /evidence="ECO:0007829|PDB:7MDS"
FT   HELIX           116..130
FT                   /evidence="ECO:0007829|PDB:7MDS"
FT   TURN            131..133
FT                   /evidence="ECO:0007829|PDB:7MDS"
FT   STRAND          134..139
FT                   /evidence="ECO:0007829|PDB:7MDS"
FT   HELIX           145..157
FT                   /evidence="ECO:0007829|PDB:7MDS"
FT   STRAND          161..166
FT                   /evidence="ECO:0007829|PDB:7MDS"
FT   HELIX           175..186
FT                   /evidence="ECO:0007829|PDB:7MDS"
FT   STRAND          191..195
FT                   /evidence="ECO:0007829|PDB:7MDS"
FT   HELIX           197..200
FT                   /evidence="ECO:0007829|PDB:7MDS"
FT   HELIX           206..213
FT                   /evidence="ECO:0007829|PDB:7MDS"
FT   STRAND          218..223
FT                   /evidence="ECO:0007829|PDB:7MDS"
FT   HELIX           227..234
FT                   /evidence="ECO:0007829|PDB:7MDS"
FT   TURN            235..237
FT                   /evidence="ECO:0007829|PDB:7MDS"
FT   STRAND          240..243
FT                   /evidence="ECO:0007829|PDB:7MDS"
FT   HELIX           245..254
FT                   /evidence="ECO:0007829|PDB:7MDS"
FT   STRAND          259..263
FT                   /evidence="ECO:0007829|PDB:7MDS"
FT   HELIX           264..266
FT                   /evidence="ECO:0007829|PDB:7MDS"
FT   HELIX           269..277
FT                   /evidence="ECO:0007829|PDB:7MDS"
FT   HELIX           282..295
FT                   /evidence="ECO:0007829|PDB:7MDS"
FT   STRAND          297..299
FT                   /evidence="ECO:0007829|PDB:7MDS"
FT   HELIX           302..310
FT                   /evidence="ECO:0007829|PDB:7MDS"
FT   STRAND          316..319
FT                   /evidence="ECO:0007829|PDB:7MDS"
FT   HELIX           327..340
FT                   /evidence="ECO:0007829|PDB:7MDS"
FT   HELIX           342..344
FT                   /evidence="ECO:0007829|PDB:7MDS"
FT   STRAND          345..349
FT                   /evidence="ECO:0007829|PDB:7MDS"
FT   HELIX           356..358
FT                   /evidence="ECO:0007829|PDB:7MDS"
FT   STRAND          360..363
FT                   /evidence="ECO:0007829|PDB:7MDS"
SQ   SEQUENCE   365 AA;  40620 MW;  F07BBAE68F004484 CRC64;
     MSALKNYGLI SIDSALHFPR SNQLQSYKRR NAKWVSPIAA VVPNFHLPMR SLEDKNRTNT
     DDIRSLRVIT AIKTPYLPDG RFDLQAYDDL VNTQIENGAE GVIVGGTTGE GQLMSWDEHI
     MLIGHTVNCF GGRIKVIGNT GSNSTREAIH ATEQGFAMGM HGALHINPYY GKTSIEGMNA
     HFQTVLHMGP TIIYNVPGRT CQDIPPQVIF KLSQNPNMAG VKECVGNNRV EEYTEKGIVV
     WSGNDDQCHD SRWDHGATGV ISVTSNLVPG LMRKLMFEGR NSALNAKLLP LMDWLFQEPN
     PIGVNTALAQ LGVARPVFRL PYVPLPLSKR IEFVKLVKEI GREHFVGDRD VQVLDDDDFI
     LIGRY
//