PKSA_ARATH
ID PKSA_ARATH Reviewed; 395 AA.
AC O23674; Q4JNW9;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Type III polyketide synthase A {ECO:0000303|PubMed:19043200};
DE Short=PKS-A;
DE EC=2.3.1.- {ECO:0000305|PubMed:19043200};
DE AltName: Full=Hydroxyalkyl alpha-pyrone synthase PKS-A {ECO:0000303|PubMed:21193570};
DE AltName: Full=Protein LESS ADHESIVE POLLEN 6 {ECO:0000303|PubMed:20442277};
GN Name=PKSA {ECO:0000303|PubMed:19043200};
GN Synonyms=LAP6 {ECO:0000312|EMBL:AEE27371.1};
GN OrderedLocusNames=At1g02050 {ECO:0000312|Araport:AT1G02050};
GN ORFNames=T7I23.4 {ECO:0000312|EMBL:AAC24368.1};
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 {ECO:0000312|Proteomes:UP000006548};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-392.
RC STRAIN=cv. Ag-0, cv. Ba-1, cv. En-T, cv. Gr-1, cv. Gre-0, cv. Lip-0,
RC cv. Litva, cv. Mv-0, cv. Oy-0, cv. Rs-1, and cv. St-0;
RX PubMed=17611127; DOI=10.1016/j.ympev.2007.05.006;
RA Wang W.-K., Schaal B.A., Chiou Y.-M., Murakami N., Ge X.-J., Huang C.-C.,
RA Chiang T.-Y.;
RT "Diverse selective modes among orthologs/paralogs of the chalcone synthase
RT (Chs) gene family of Arabidopsis thaliana and its relative A. halleri ssp.
RT gemmifera.";
RL Mol. Phylogenet. Evol. 44:503-520(2007).
RN [5]
RP FUNCTION, NOMENCLATURE, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19043200; DOI=10.1248/bpb.31.2205;
RA Mizuuchi Y., Shimokawa Y., Wanibuchi K., Noguchi H., Abe I.;
RT "Structure function analysis of novel type III polyketide synthases from
RT Arabidopsis thaliana.";
RL Biol. Pharm. Bull. 31:2205-2210(2008).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=21193570; DOI=10.1105/tpc.110.080028;
RA Kim S.S., Grienenberger E., Lallemand B., Colpitts C.C., Kim S.Y.,
RA de Azevedo Souza C., Geoffroy P., Heintz D., Krahn D., Kaiser M.,
RA Kombrink E., Heitz T., Suh D.-Y., Legrand M., Douglas C.J.;
RT "LAP6/POLYKETIDE SYNTHASE A and LAP5/POLYKETIDE SYNTHASE B encode
RT hydroxyalkyl alpha-pyrone synthases required for pollen development and
RT sporopollenin biosynthesis in Arabidopsis thaliana.";
RL Plant Cell 22:4045-4066(2010).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ILE-132, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND GENE FAMILY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=20442277; DOI=10.1104/pp.110.157446;
RA Dobritsa A.A., Lei Z., Nishikawa S., Urbanczyk-Wochniak E., Huhman D.V.,
RA Preuss D., Sumner L.W.;
RT "LAP5 and LAP6 encode anther-specific proteins with similarity to chalcone
RT synthase essential for pollen exine development in Arabidopsis.";
RL Plant Physiol. 153:937-955(2010).
RN [8]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH 4CLL1/ACOS5
RP AND TKPR1.
RX PubMed=23632852; DOI=10.1104/pp.112.213124;
RA Lallemand B., Erhardt M., Heitz T., Legrand M.;
RT "Sporopollenin biosynthetic enzymes interact and constitute a metabolon
RT localized to the endoplasmic reticulum of tapetum cells.";
RL Plant Physiol. 162:616-625(2013).
CC -!- FUNCTION: Plant type III polyketide synthases (PKSs) that catalyzes the
CC condensation of malonyl-CoA units with various CoA ester starter
CC molecules to generate a diverse array of natural products including
CC long-chain alkyl alpha-pyrones. Accepts up to C(20) chain-length fatty
CC acyl CoAs as starter substrates, and carries out sequential
CC condensations with malonyl-CoA to produce triketide and tetraketide
CC alpha-pyrones, potential sporopollenin precursors (PubMed:19043200,
CC PubMed:21193570). Favorite substrates for are midchain- and v-
CC hydroxylated fatty acyl-CoAs (e.g. 12-hydroxyoctadecanoyl-CoA and 16-
CC hydroxyhexadecanoyl-CoA). Required for pollen development and
CC sporopollenin biosynthesis, the major constituent of exine in the outer
CC pollen wall (PubMed:21193570, PubMed:20442277). In vitro, can use 4-
CC coumaroyl-coenzyme A as substrate to produce bis-noryangonin and fatty
CC acyl-coenzyme A as substrate to produce medium-chain alkyl pyrones. May
CC play a role in both the synthesis of pollen fatty acids and phenolics
CC found in exine (PubMed:20442277). {ECO:0000269|PubMed:19043200,
CC ECO:0000269|PubMed:20442277, ECO:0000269|PubMed:21193570}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=22.9 uM for n-dodecanoyl-CoA (at pH 7 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:19043200};
CC KM=25 uM for 16-OH-C16-CoA {ECO:0000269|PubMed:21193570};
CC KM=23 uM for 12-OH-C18-CoA {ECO:0000269|PubMed:21193570};
CC KM=48 uM for C16-CoA {ECO:0000269|PubMed:21193570};
CC Note=kcat is 0.11 min(-1) with n-dodecanoyl-CoA as substrate for the
CC production of the triketide alpha-pyrone (at pH 7 and 30 degrees
CC Celsius)(PubMed:19043200). kcat is 2.8 msec(-1) with 16-OH-C16-CoA as
CC substrate, 5 msec(-1) with 12-OH-C18-CoA as substrate and 0.13 msec(-
CC 1) with C16-CoA as substrate (PubMed:21193570).
CC {ECO:0000269|PubMed:19043200, ECO:0000269|PubMed:21193570};
CC pH dependence:
CC Optimum pH is 7 (at 30 degrees Celsius).
CC {ECO:0000269|PubMed:19043200};
CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC {ECO:0000250|UniProtKB:Q9LKP7}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with 4CLL1/ACOS5 and
CC TKPR1 (PubMed:23632852). {ECO:0000250|UniProtKB:P30074,
CC ECO:0000269|PubMed:23632852}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:21193570, ECO:0000269|PubMed:23632852}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers and flower buds (at protein
CC level), and, at very low levels, in roots, seedlings, leaves and stems
CC (PubMed:21193570, PubMed:20442277). Mostly confined to anther tapetal
CC cells (PubMed:23632852). {ECO:0000269|PubMed:20442277,
CC ECO:0000269|PubMed:21193570, ECO:0000269|PubMed:23632852}.
CC -!- DEVELOPMENTAL STAGE: Most abundant in the youngest flower buds, but
CC levels decline as flowers mature. Specifically and transiently
CC expressed in tapetal cells during microspore development in anthers (at
CC protein level). {ECO:0000269|PubMed:20442277,
CC ECO:0000269|PubMed:21193570}.
CC -!- DISRUPTION PHENOTYPE: Pollen exine layer defects. Reduced accumulation
CC of flavonoid precursors and flavonoids in developing anthers. Plants
CC lacking both PKS-A and PKS-B are completely male sterile, with no
CC apparent exine, thus leading to pollen grain collapse under vacuum.
CC Altered pollen-stigma adhesion. {ECO:0000269|PubMed:20442277,
CC ECO:0000269|PubMed:21193570}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
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DR EMBL; U89959; AAC24368.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27371.1; -; Genomic_DNA.
DR EMBL; BT030313; ABO09877.1; -; mRNA.
DR EMBL; DQ062309; AAY96717.1; -; Genomic_DNA.
DR EMBL; DQ062310; AAY96718.1; -; Genomic_DNA.
DR EMBL; DQ062318; AAY96726.1; -; Genomic_DNA.
DR EMBL; DQ062322; AAY96730.1; -; Genomic_DNA.
DR EMBL; DQ062323; AAY96731.1; -; Genomic_DNA.
DR EMBL; DQ062324; AAY96732.1; -; Genomic_DNA.
DR EMBL; DQ062327; AAY96735.1; -; Genomic_DNA.
DR EMBL; DQ062328; AAY96736.1; -; Genomic_DNA.
DR EMBL; DQ062331; AAY96739.1; -; Genomic_DNA.
DR EMBL; DQ062336; AAY96744.1; -; Genomic_DNA.
DR EMBL; DQ062339; AAY96747.1; -; Genomic_DNA.
DR PIR; E86152; E86152.
DR RefSeq; NP_171707.1; NM_100085.4.
DR AlphaFoldDB; O23674; -.
DR SMR; O23674; -.
DR STRING; 3702.AT1G02050.1; -.
DR PaxDb; O23674; -.
DR PRIDE; O23674; -.
DR EnsemblPlants; AT1G02050.1; AT1G02050.1; AT1G02050.
DR GeneID; 839280; -.
DR Gramene; AT1G02050.1; AT1G02050.1; AT1G02050.
DR KEGG; ath:AT1G02050; -.
DR Araport; AT1G02050; -.
DR TAIR; locus:2205588; AT1G02050.
DR eggNOG; ENOG502QSSY; Eukaryota.
DR HOGENOM; CLU_034992_2_0_1; -.
DR InParanoid; O23674; -.
DR OMA; GQESPFM; -.
DR OrthoDB; 950070at2759; -.
DR PhylomeDB; O23674; -.
DR BioCyc; ARA:AT1G02050-MON; -.
DR BioCyc; MetaCyc:AT1G02050-MON; -.
DR UniPathway; UPA00154; -.
DR PRO; PR:O23674; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O23674; baseline and differential.
DR Genevisible; O23674; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IBA:GO_Central.
DR GO; GO:0090439; F:tetraketide alpha-pyrone synthase activity; IDA:TAIR.
DR GO; GO:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0010584; P:pollen exine formation; IMP:TAIR.
DR GO; GO:0030639; P:polyketide biosynthetic process; IDA:TAIR.
DR GO; GO:0080110; P:sporopollenin biosynthetic process; IMP:TAIR.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR012328; Chalcone/stilbene_synt_C.
DR InterPro; IPR001099; Chalcone/stilbene_synt_N.
DR InterPro; IPR011141; Polyketide_synthase_type-III.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR11877; PTHR11877; 1.
DR Pfam; PF02797; Chal_sti_synt_C; 1.
DR Pfam; PF00195; Chal_sti_synt_N; 1.
DR PIRSF; PIRSF000451; PKS_III; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
PE 1: Evidence at protein level;
KW Acyltransferase; Developmental protein; Endoplasmic reticulum;
KW Flavonoid biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..395
FT /note="Type III polyketide synthase A"
FT /id="PRO_0000432840"
FT ACT_SITE 172
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q94FV7,
FT ECO:0000255|PROSITE-ProRule:PRU10023"
FT BINDING 63..70
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P30074"
FT BINDING 224..225
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30074"
FT BINDING 274
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q58VP7"
FT BINDING 314..317
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q58VP7"
FT BINDING 317
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P30074"
FT MUTAGEN 132
FT /note="I->T: In lap6-1; pollen exine layer defects leading
FT to altered pollen-stigma adhesion."
FT /evidence="ECO:0000269|PubMed:20442277"
SQ SEQUENCE 395 AA; 43617 MW; C9DC274EEF0C6461 CRC64;
MSNSRMNGVE KLSSKSTRRV ANAGKATLLA LGKAFPSQVV PQENLVEGFL RDTKCDDAFI
KEKLEHLCKT TTVKTRYTVL TREILAKYPE LTTEGSPTIK QRLEIANEAV VEMALEASLG
CIKEWGRPVE DITHIVYVSS SEIRLPGGDL YLSAKLGLRN DVNRVMLYFL GCYGGVTGLR
VAKDIAENNP GSRVLLTTSE TTILGFRPPN KARPYDLVGA ALFGDGAAAV IIGADPRECE
APFMELHYAV QQFLPGTQNV IEGRLTEEGI NFKLGRDLPQ KIEENIEEFC KKLMGKAGDE
SMEFNDMFWA VHPGGPAILN RLETKLKLEK EKLESSRRAL VDYGNVSSNT ILYVMEYMRD
ELKKKGDAAQ EWGLGLAFGP GITFEGLLIR SLTSS
