PKSB_ARATH
ID PKSB_ARATH Reviewed; 392 AA.
AC Q8LDM2; A0MFB8; Q9SW49;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Type III polyketide synthase B {ECO:0000303|PubMed:19043200};
DE Short=PKS-B;
DE EC=2.3.1.- {ECO:0000305|PubMed:19043200};
DE AltName: Full=Hydroxyalkyl alpha-pyrone synthase PKS-B {ECO:0000303|PubMed:21193570};
DE AltName: Full=Protein LESS ADHESIVE POLLEN 5 {ECO:0000303|PubMed:20442277};
GN Name=PKSB {ECO:0000303|PubMed:19043200};
GN Synonyms=LAP5 {ECO:0000312|EMBL:AEE86428.1};
GN OrderedLocusNames=At4g34850 {ECO:0000312|Araport:AT4G34850};
GN ORFNames=T11I11.90 {ECO:0000312|EMBL:CAB45446.1};
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 [MRNA].
RC STRAIN=cv. Ag-0, cv. Ba-1, cv. Bl-1, cv. Bla-1, cv. Br-0, cv. Can-0,
RC cv. Chi-0, cv. Co-1, cv. En-D, cv. En-T, cv. Es-0, cv. Gr-1, cv. Ita-0,
RC cv. Kin-0, cv. Lip-0, cv. Mt-0, cv. Mv-0, cv. Pog-0, cv. Ri-0, cv. Rs-1,
RC cv. St-0, cv. Tsu-0, cv. Van-0, and cv. Yo-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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [6]
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 [7]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY,
RP 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 [8]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-227, 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 [9]
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=30.4 uM for n-dodecanoyl-CoA (at pH 7 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:19043200};
CC Note=kcat is 0.06 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). {ECO:0000269|PubMed:19043200};
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) (PubMed:21193570, PubMed:20442277). Mostly confined to anther
CC tapetal 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28665.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; DQ062353; AAZ23694.1; -; mRNA.
DR EMBL; DQ062354; AAZ23695.1; -; mRNA.
DR EMBL; DQ062355; AAZ23696.1; -; mRNA.
DR EMBL; DQ062356; AAZ23697.1; -; mRNA.
DR EMBL; DQ062357; AAZ23698.1; -; mRNA.
DR EMBL; DQ062359; AAZ23700.1; -; mRNA.
DR EMBL; DQ062360; AAZ23701.1; -; mRNA.
DR EMBL; DQ062362; AAZ23703.1; -; mRNA.
DR EMBL; DQ062365; AAZ23706.1; -; mRNA.
DR EMBL; DQ062366; AAZ23707.1; -; mRNA.
DR EMBL; DQ062369; AAZ23710.1; -; mRNA.
DR EMBL; DQ062370; AAZ23711.1; -; mRNA.
DR EMBL; DQ062371; AAZ23712.1; -; mRNA.
DR EMBL; DQ062372; AAZ23713.1; -; mRNA.
DR EMBL; DQ062373; AAZ23714.1; -; mRNA.
DR EMBL; DQ062374; AAZ23715.1; -; mRNA.
DR EMBL; DQ062375; AAZ23716.1; -; mRNA.
DR EMBL; DQ062377; AAZ23718.1; -; mRNA.
DR EMBL; DQ062378; AAZ23719.1; -; mRNA.
DR EMBL; DQ062379; AAZ23720.1; -; mRNA.
DR EMBL; DQ062381; AAZ23722.1; -; mRNA.
DR EMBL; DQ062382; AAZ23723.1; -; mRNA.
DR EMBL; DQ062383; AAZ23724.1; -; mRNA.
DR EMBL; DQ062384; AAZ23725.1; -; mRNA.
DR EMBL; AL079347; CAB45446.1; -; Genomic_DNA.
DR EMBL; AL161586; CAB80202.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86428.1; -; Genomic_DNA.
DR EMBL; DQ446894; ABE66111.1; -; mRNA.
DR EMBL; DQ653244; ABK28665.1; ALT_SEQ; mRNA.
DR EMBL; AY085918; AAM63130.1; -; mRNA.
DR PIR; T10231; T10231.
DR RefSeq; NP_567971.1; NM_119651.4.
DR AlphaFoldDB; Q8LDM2; -.
DR SMR; Q8LDM2; -.
DR STRING; 3702.AT4G34850.1; -.
DR PaxDb; Q8LDM2; -.
DR PRIDE; Q8LDM2; -.
DR EnsemblPlants; AT4G34850.1; AT4G34850.1; AT4G34850.
DR GeneID; 829637; -.
DR Gramene; AT4G34850.1; AT4G34850.1; AT4G34850.
DR KEGG; ath:AT4G34850; -.
DR Araport; AT4G34850; -.
DR TAIR; locus:2116845; AT4G34850.
DR eggNOG; ENOG502QSSY; Eukaryota.
DR HOGENOM; CLU_034992_2_0_1; -.
DR InParanoid; Q8LDM2; -.
DR OrthoDB; 950070at2759; -.
DR PhylomeDB; Q8LDM2; -.
DR BioCyc; ARA:AT4G34850-MON; -.
DR BioCyc; MetaCyc:AT4G34850-MON; -.
DR UniPathway; UPA00154; -.
DR PRO; PR:Q8LDM2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8LDM2; baseline and differential.
DR Genevisible; Q8LDM2; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
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..392
FT /note="Type III polyketide synthase B"
FT /id="PRO_0000432841"
FT ACT_SITE 166
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q94FV7,
FT ECO:0000255|PROSITE-ProRule:PRU10023"
FT BINDING 57..64
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P30074"
FT BINDING 218..219
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30074"
FT BINDING 269
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q58VP7"
FT BINDING 309..312
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q58VP7"
FT BINDING 312
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P30074"
FT MUTAGEN 227
FT /note="G->E: In lap5-1; pollen exine layer defects leading
FT to altered pollen-stigma adhesion."
FT /evidence="ECO:0000269|PubMed:20442277"
FT CONFLICT 61..62
FT /note="Missing (in Ref. 2; CAB45446/CAB80202)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 392 AA; 42982 MW; 4CA0E86BECD19D2E CRC64;
MGSIDAAVLG SEKKSNPGKA TILALGKAFP HQLVMQEYLV DGYFKTTKCD DPELKQKLTR
LCKTTTVKTR YVVMSEEILK KYPELAIEGG STVTQRLDIC NDAVTEMAVE ASRACIKNWG
RSISDITHVV YVSSSEARLP GGDLYLAKGL GLSPDTHRVL LYFVGCSGGV AGLRVAKDIA
ENNPGSRVLL ATSETTIIGF KPPSVDRPYD LVGVALFGDG AGAMIIGSDP DPICEKPLFE
LHTAIQNFLP ETEKTIDGRL TEQGINFKLS RELPQIIEDN VENFCKKLIG KAGLAHKNYN
QMFWAVHPGG PAILNRIEKR LNLSPEKLSP SRRALMDYGN ASSNSIVYVL EYMLEESKKV
RNMNEEENEW GLILAFGPGV TFEGIIARNL DV
