ID DAPA2_ARATH Reviewed; 365 AA. AC Q9FVC8; O22129; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 20-JUN-2001, sequence version 2. DT 27-MAR-2024, entry version 150. DE RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase 2, chloroplastic; DE Short=HTPA synthase 2; DE EC=4.3.3.7; DE Flags: Precursor; GN Name=DHDPS2; OrderedLocusNames=At2g45440; ORFNames=F4L23.5; 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 [GENOMIC DNA]. RC STRAIN=cv. Wassilewskija; RX PubMed=11069709; DOI=10.1046/j.1365-313x.2000.00884.x; RA Sarrobert C., Thibaud M.-C., Contard-David P., Gineste S., Bechtold N., RA Robaglia C., Nussaume L.; RT "Identification of an Arabidopsis thaliana mutant accumulating threonine RT resulting from mutation in a new dihydrodipicolinate synthase gene."; RL Plant J. 24:357-367(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10617197; DOI=10.1038/45471; RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."; RL Nature 402:761-768(1999). 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]. 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). 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 -!- 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF200325; AAG28565.1; -; Genomic_DNA. DR EMBL; AC002387; AAB82620.1; -; Genomic_DNA. DR EMBL; CP002685; AEC10554.1; -; Genomic_DNA. DR EMBL; BT004823; AAO44089.1; -; mRNA. DR PIR; E84890; E84890. DR RefSeq; NP_182068.1; NM_130106.3. DR PDB; 4DPP; X-ray; 2.00 A; A/B=39-365. DR PDB; 4DPQ; X-ray; 2.20 A; A/B=39-365. DR PDBsum; 4DPP; -. DR PDBsum; 4DPQ; -. DR AlphaFoldDB; Q9FVC8; -. DR SMR; Q9FVC8; -. DR BioGRID; 4488; 4. DR STRING; 3702.Q9FVC8; -. DR PaxDb; 3702-AT2G45440-1; -. DR ProteomicsDB; 222756; -. DR EnsemblPlants; AT2G45440.1; AT2G45440.1; AT2G45440. DR GeneID; 819152; -. DR Gramene; AT2G45440.1; AT2G45440.1; AT2G45440. DR KEGG; ath:AT2G45440; -. DR Araport; AT2G45440; -. DR TAIR; AT2G45440; DHDPS2. DR eggNOG; ENOG502QQ8M; Eukaryota. DR HOGENOM; CLU_049343_3_0_1; -. DR InParanoid; Q9FVC8; -. DR OMA; ALCAMIT; -. DR OrthoDB; 1780992at2759; -. DR PhylomeDB; Q9FVC8; -. DR BioCyc; ARA:AT2G45440-MONOMER; -. DR BRENDA; 4.3.3.7; 399. DR UniPathway; UPA00034; UER00017. DR PRO; PR:Q9FVC8; -. DR Proteomes; UP000006548; Chromosome 2. DR ExpressionAtlas; Q9FVC8; baseline and differential. DR GO; GO:0009507; C:chloroplast; HDA:TAIR. DR GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IDA:CACAO. 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:SF71; 4-HYDROXY-TETRAHYDRODIPICOLINATE SYNTHASE 2, 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; Q9FVC8; AT. PE 1: Evidence at protein level; KW 3D-structure; Allosteric enzyme; Amino-acid biosynthesis; Chloroplast; KW Diaminopimelate biosynthesis; Lyase; Lysine biosynthesis; Plastid; KW Reference proteome; Schiff base; Transit peptide. FT TRANSIT 1..39 FT /note="Chloroplast" FT /evidence="ECO:0000255" FT CHAIN 40..365 FT /note="4-hydroxy-tetrahydrodipicolinate synthase 2, FT chloroplastic" FT /id="PRO_0000007198" 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 CONFLICT 26 FT /note="S -> G (in Ref. 1; AAG28565)" FT /evidence="ECO:0000305" FT HELIX 60..64 FT /evidence="ECO:0007829|PDB:4DPP" FT STRAND 68..71 FT /evidence="ECO:0007829|PDB:4DPP" FT STRAND 80..82 FT /evidence="ECO:0007829|PDB:4DPP" FT HELIX 84..96 FT /evidence="ECO:0007829|PDB:4DPP" FT STRAND 101..106 FT /evidence="ECO:0007829|PDB:4DPP" FT TURN 107..110 FT /evidence="ECO:0007829|PDB:4DPP" FT HELIX 111..113 FT /evidence="ECO:0007829|PDB:4DPP" FT HELIX 116..130 FT /evidence="ECO:0007829|PDB:4DPP" FT TURN 131..133 FT /evidence="ECO:0007829|PDB:4DPP" FT STRAND 134..139 FT /evidence="ECO:0007829|PDB:4DPP" FT HELIX 145..157 FT /evidence="ECO:0007829|PDB:4DPP" FT STRAND 161..166 FT /evidence="ECO:0007829|PDB:4DPP" FT HELIX 175..183 FT /evidence="ECO:0007829|PDB:4DPP" FT HELIX 186..188 FT /evidence="ECO:0007829|PDB:4DPP" FT STRAND 191..195 FT /evidence="ECO:0007829|PDB:4DPP" FT HELIX 197..200 FT /evidence="ECO:0007829|PDB:4DPP" FT HELIX 206..212 FT /evidence="ECO:0007829|PDB:4DPP" FT STRAND 218..223 FT /evidence="ECO:0007829|PDB:4DPP" FT HELIX 227..235 FT /evidence="ECO:0007829|PDB:4DPP" FT STRAND 240..242 FT /evidence="ECO:0007829|PDB:4DPP" FT HELIX 245..247 FT /evidence="ECO:0007829|PDB:4DPP" FT HELIX 248..254 FT /evidence="ECO:0007829|PDB:4DPP" FT STRAND 259..263 FT /evidence="ECO:0007829|PDB:4DPP" FT HELIX 264..266 FT /evidence="ECO:0007829|PDB:4DPP" FT HELIX 269..277 FT /evidence="ECO:0007829|PDB:4DPP" FT HELIX 282..295 FT /evidence="ECO:0007829|PDB:4DPP" FT STRAND 297..299 FT /evidence="ECO:0007829|PDB:4DPP" FT HELIX 302..310 FT /evidence="ECO:0007829|PDB:4DPP" FT STRAND 316..319 FT /evidence="ECO:0007829|PDB:4DPP" FT HELIX 327..340 FT /evidence="ECO:0007829|PDB:4DPP" FT HELIX 342..344 FT /evidence="ECO:0007829|PDB:4DPP" FT STRAND 345..349 FT /evidence="ECO:0007829|PDB:4DPP" FT HELIX 356..358 FT /evidence="ECO:0007829|PDB:4DPP" FT STRAND 360..363 FT /evidence="ECO:0007829|PDB:4DPP" SQ SEQUENCE 365 AA; 40292 MW; 43BECEF1FC3E557A CRC64; MAALKGYGLC SMDSALQFPC PKLFNSYKRR SSKWVSPKAA VVPNFHLPMR SLEVKNRTNT DDIKALRVIT AIKTPYLPDG RFDLEAYDDL VNIQIQNGAE GVIVGGTTGE GQLMSWDEHI MLIGHTVNCF GGSIKVIGNT GSNSTREAIH ATEQGFAVGM HAALHINPYY GKTSIEGLIA HFQSVLHMGP TIIYNVPGRT GQDIPPRAIF KLSQNPNLAG VKECVGNKRV EEYTENGVVV WSGNDDECHD SRWDYGATGV ISVTSNLVPG LMRKLMFEGR NSSLNSKLLP LMAWLFHEPN PIGINTALAQ LGVSRPVFRL PYVPLPLSKR LEFVKLVKEI GREHFVGEKD VQALDDDDFI LIGRY //