ID   KDSA2_ARATH             Reviewed;         291 AA.
AC   Q6NQL4; Q9SA33;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   02-SEP-2026, entry version 141.
DE   RecName: Full=2-dehydro-3-deoxyphosphooctonate aldolase 2;
DE            EC=2.5.1.55 {ECO:0000250|UniProtKB:Q9AV97};
DE   AltName: Full=3-deoxy-D-manno-octulosonic acid 8-phosphate synthase;
DE   AltName: Full=KDO-8-phosphate synthase 2;
DE            Short=AtkdsA2;
DE            Short=KDO 8-P synthase;
DE            Short=KDOPS;
DE   AltName: Full=Phospho-2-dehydro-3-deoxyoctonate aldolase;
GN   Name=KDSA2; Synonyms=kdsA; OrderedLocusNames=At1g16340;
GN   ORFNames=F3O9.14;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
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   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
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).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=18503041; DOI=10.1093/jxb/ern118;
RA   Delmas F., Seveno M., Northey J.G., Hernould M., Lerouge P., McCourt P.,
RA   Chevalier C.;
RT   "The synthesis of the rhamnogalacturonan II component 3-deoxy-D-manno-2-
RT   octulosonic acid (Kdo) is required for pollen tube growth and elongation.";
RL   J. Exp. Bot. 59:2639-2647(2008).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC   -!- FUNCTION: Catalyzes the stereospecific condensation of D-arabinose 5-
CC       phosphate and phosphoenolpyruvate to form 3-deoxy-D-manno-octulosonate
CC       8-phosphate (KDO-8-phosphate) and inorganic phosphate. Involved in the
CC       biosynthesis of 3-deoxy-D-manno-octulosonate (KDO) which is an
CC       indispensable component of rhamnogalacturonan II (RG-II), a
CC       structurally complex pectic polysaccharide of the primary cell wall.
CC       RG-II is essential for the cell wall integrity of rapidly growing
CC       tissues and pollen tube growth and elongation.
CC       {ECO:0000269|PubMed:18503041}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-arabinose 5-phosphate + phosphoenolpyruvate + H2O = 3-deoxy-
CC         alpha-D-manno-2-octulosonate-8-phosphate + phosphate;
CC         Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985; EC=2.5.1.55;
CC         Evidence={ECO:0000250|UniProtKB:Q9AV97};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU01406}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q6NQL4-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed in roots, apical meristem, emerging
CC       leaves, hydathodes of young leaves, styles of mature flowers and
CC       funicules of mature siliques. {ECO:0000269|PubMed:18503041}.
CC   -!- SIMILARITY: Belongs to the class-I DAHP synthase family. KdsA
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01406}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD34685.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC006341; AAD34685.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE29437.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE29438.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE29439.1; -; Genomic_DNA.
DR   EMBL; OZ408683; CAO7027577.1; -; Genomic_DNA.
DR   EMBL; BT010438; AAQ62439.1; -; mRNA.
DR   EMBL; AK175407; BAD43170.1; -; mRNA.
DR   PIR; E86298; E86298.
DR   RefSeq; NP_001031055.1; NM_001035978.2. [Q6NQL4-1]
DR   RefSeq; NP_001077547.1; NM_001084078.1. [Q6NQL4-1]
DR   RefSeq; NP_173084.1; NM_101500.4. [Q6NQL4-1]
DR   AlphaFoldDB; Q6NQL4; -.
DR   SMR; Q6NQL4; -.
DR   BioGRID; 23443; 1.
DR   FunCoup; Q6NQL4; 366.
DR   STRING; 3702.Q6NQL4; -.
DR   iPTMnet; Q6NQL4; -.
DR   MetOSite; Q6NQL4; -.
DR   PaxDb; 3702-Q6NQL4; -.
DR   ProteomicsDB; 250757; -. [Q6NQL4-1]
DR   GeneID; 838203; -.
DR   KEGG; ath:AT1G16340; -.
DR   Araport; AT1G16340; -.
DR   TAIR; AT1G16340; ATKDSA2.
DR   eggNOG; ENOG502QQN7; Eukaryota.
DR   InParanoid; Q6NQL4; -.
DR   PhylomeDB; Q6NQL4; -.
DR   BioCyc; ARA:AT1G16340-MONOMER; -.
DR   BRENDA; 2.5.1.55; 399.
DR   PRO; PR:Q6NQL4; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q6NQL4; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISM:TAIR.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008676; F:3-deoxy-8-phosphooctulonate synthase activity; IDA:UniProtKB.
DR   GO; GO:0046364; P:monosaccharide biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0048868; P:pollen tube development; IMP:UniProtKB.
DR   GO; GO:0009860; P:pollen tube growth; IMP:UniProtKB.
DR   GO; GO:0010306; P:rhamnogalacturonan II biosynthetic process; TAS:UniProtKB.
DR   FunFam; 3.20.20.70:FF:000254; 2-dehydro-3-deoxyphosphooctonate aldolase 2; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_00056; KDO8P_synth; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006218; DAHP1/KDSA.
DR   InterPro; IPR006269; KDO8P_synthase.
DR   NCBIfam; TIGR01362; KDO8P_synth; 1.
DR   NCBIfam; NF003543; PRK05198.1; 1.
DR   PANTHER; PTHR21057; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE; 1.
DR   Pfam; PF00793; DAHP_synth_1; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS52061; DAHPS_I; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell wall biogenesis/degradation;
KW   Cytoplasm; Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..291
FT                   /note="2-dehydro-3-deoxyphosphooctonate aldolase 2"
FT                   /id="PRO_0000421463"
FT   DOMAIN          15..276
FT                   /note="DAHPS class-I TIM-barrel"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01406"
FT   BINDING         54
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01406"
FT   BINDING         59
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01406"
FT   BINDING         137
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01406"
FT   BINDING         167
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01406"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
SQ   SEQUENCE   291 AA;  31676 MW;  E0EEC13A56AD9FAC CRC64;
     MANSASLLYD QLKVAEPFFL LAGPNVIESE EHVLRMAKSI KDISTKLGLP LVFKSSFDKA
     NRTSSKSFRG PGMAEGLKIL EKVKVAFDLP IVTDVHESSQ CEAVGKVADI IQIPAFLCRQ
     TDLLVAAAQS GKIINIKKGQ FCGHSVMRNS AEKVRLAGNP NVMVCERGTM FGYNDLIVDP
     RNLEWMREAD CPVVADITHS LQQPAGKKLD GGGVASGGLR ELIPCIARTA VAVGVDGIFM
     EVHDDPLNAP VDGPTQWPLR HLEELLEELI AIASVTKGKQ QFQIDLTPYR D
//