KDSA1_ARATH
ID KDSA1_ARATH Reviewed; 290 AA.
AC Q9AV97; B9DG45; Q8L890; Q9SAJ9;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=2-dehydro-3-deoxyphosphooctonate aldolase 1;
DE EC=2.5.1.55 {ECO:0000269|PubMed:12754267, ECO:0000269|PubMed:15070398};
DE AltName: Full=3-deoxy-D-manno-octulosonic acid 8-phosphate synthase;
DE AltName: Full=KDO-8-phosphate synthase 1;
DE Short=AtkdsA1;
DE Short=KDO 8-P synthase;
DE Short=KDOPS;
DE AltName: Full=Phospho-2-dehydro-3-deoxyoctonate aldolase;
GN Name=KDSA1; OrderedLocusNames=At1g79500; ORFNames=T8K14.8;
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], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RX PubMed=12754267; DOI=10.1093/jxb/erg181;
RA Matsuura K., Miyagawa I., Kobayashi M., Ohta D., Matoh T.;
RT "Arabidopsis 3-deoxy-D-manno-oct-2-ulosonate-8-phosphate synthase: cDNA
RT cloning and expression analyses.";
RL J. Exp. Bot. 54:1785-1787(2003).
RN [2]
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 [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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15070398; DOI=10.1042/bj20040207;
RA Wu J., Patel M.A., Sundaram A.K., Woodard R.W.;
RT "Functional and biochemical characterization of a recombinant Arabidopsis
RT thaliana 3-deoxy-D-manno-octulosonate 8-phosphate synthase.";
RL Biochem. J. 381:185-193(2004).
RN [7]
RP FUNCTION.
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 [8]
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:12754267, ECO:0000269|PubMed:15070398,
CC ECO:0000269|PubMed:18503041}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 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:0000269|PubMed:12754267, ECO:0000269|PubMed:15070398};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.6 uM for phosphoenolpyruvate {ECO:0000269|PubMed:15070398};
CC KM=3.8 uM for D-arabinose 5-phosphate {ECO:0000269|PubMed:15070398};
CC pH dependence:
CC Optimum pH is 6.5-9.5. {ECO:0000269|PubMed:15070398};
CC Temperature dependence:
CC Optimum temperature is 65 degrees Celsius.
CC {ECO:0000269|PubMed:15070398};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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=Q9AV97-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in shoots. {ECO:0000269|PubMed:12754267}.
CC -!- SIMILARITY: Belongs to the KdsA family. {ECO:0000305}.
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DR EMBL; AB059683; BAB41014.1; -; mRNA.
DR EMBL; AC007202; AAD30227.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36251.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36252.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36253.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36254.1; -; Genomic_DNA.
DR EMBL; AF372947; AAK50087.1; -; mRNA.
DR EMBL; AY113162; AAM47465.1; -; mRNA.
DR EMBL; AK317018; BAH19712.1; -; mRNA.
DR PIR; C96826; C96826.
DR RefSeq; NP_001319413.1; NM_001334882.1. [Q9AV97-1]
DR RefSeq; NP_001319414.1; NM_001334883.1. [Q9AV97-1]
DR RefSeq; NP_001319415.1; NM_001334884.1. [Q9AV97-1]
DR RefSeq; NP_178068.1; NM_106598.4. [Q9AV97-1]
DR AlphaFoldDB; Q9AV97; -.
DR SMR; Q9AV97; -.
DR BioGRID; 29507; 2.
DR iPTMnet; Q9AV97; -.
DR PaxDb; Q9AV97; -.
DR PRIDE; Q9AV97; -.
DR ProteomicsDB; 250667; -. [Q9AV97-1]
DR EnsemblPlants; AT1G79500.1; AT1G79500.1; AT1G79500. [Q9AV97-1]
DR EnsemblPlants; AT1G79500.2; AT1G79500.2; AT1G79500. [Q9AV97-1]
DR EnsemblPlants; AT1G79500.3; AT1G79500.3; AT1G79500. [Q9AV97-1]
DR EnsemblPlants; AT1G79500.4; AT1G79500.4; AT1G79500. [Q9AV97-1]
DR GeneID; 844288; -.
DR Gramene; AT1G79500.1; AT1G79500.1; AT1G79500. [Q9AV97-1]
DR Gramene; AT1G79500.2; AT1G79500.2; AT1G79500. [Q9AV97-1]
DR Gramene; AT1G79500.3; AT1G79500.3; AT1G79500. [Q9AV97-1]
DR Gramene; AT1G79500.4; AT1G79500.4; AT1G79500. [Q9AV97-1]
DR KEGG; ath:AT1G79500; -.
DR Araport; AT1G79500; -.
DR HOGENOM; CLU_036666_0_0_1; -.
DR InParanoid; Q9AV97; -.
DR OMA; FRGIPTM; -.
DR PhylomeDB; Q9AV97; -.
DR BioCyc; ARA:AT1G79500-MON; -.
DR BioCyc; MetaCyc:AT1G79500-MON; -.
DR BRENDA; 2.5.1.55; 399.
DR PRO; PR:Q9AV97; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9AV97; baseline and differential.
DR Genevisible; Q9AV97; AT.
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 Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00056; KDO8P_synth; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006218; DAHP1/KDSA.
DR InterPro; IPR006269; KDO8P_synthase.
DR PANTHER; PTHR21057; PTHR21057; 1.
DR Pfam; PF00793; DAHP_synth_1; 1.
DR TIGRFAMs; TIGR01362; KDO8P_synth; 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..290
FT /note="2-dehydro-3-deoxyphosphooctonate aldolase 1"
FT /id="PRO_0000187179"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 2
FT /note="A -> T (in Ref. 4; AAM47465)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="F -> L (in Ref. 1; BAB41014)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 290 AA; 31657 MW; 2C79A24D66D4FACB CRC64;
MAATSLLYNQ LKAAEPFFLL AGPNVIESEE HILRMAKHIK DISTKVGLPL VFKSSFDKAN
RTSSKSFRGP GMAEGLKILE KVKVAYDLPI VTDVHESSQC EAVGKVADII QIPAFLCRQT
DLLVAAAQTG KIINIKKGQF CAPSVMENSA EKIRLAGNPN VMVCERGTMF GYNDLIVDPR
NFEWMREANC PVVADITHSL QQPAGKKLDG GGVASGGLRE LIPCIARTAV AVGVDGIFME
VHDDPLSAPV DGPTQWPLRH LEELLEELIA IARVTKGKQR LQIDLTPYRD
