DAPA2_ARATH
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 03-AUG-2022, entry version 143.
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-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; 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.AT2G45440.1; -.
DR PaxDb; Q9FVC8; -.
DR PRIDE; Q9FVC8; -.
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; locus:2050936; AT2G45440.
DR eggNOG; ENOG502QQ8M; Eukaryota.
DR HOGENOM; CLU_049343_3_0_1; -.
DR InParanoid; Q9FVC8; -.
DR OMA; ALCAMIT; -.
DR OrthoDB; 1238597at2759; -.
DR PhylomeDB; Q9FVC8; -.
DR BioCyc; ARA:AT2G45440-MON; -.
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 Genevisible; Q9FVC8; AT.
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; -; 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 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 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
