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Type III polyketide synthase B (PKS-B) (EC 2.3.1.-) (Hydroxyalkyl alpha-pyrone synthase PKS-B) (Protein LESS ADHESIVE POLLEN 5)

 PKSB_ARATH              Reviewed;         392 AA.
Q8LDM2; A0MFB8; Q9SW49;
29-APR-2015, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
25-APR-2018, entry version 113.
RecName: Full=Type III polyketide synthase B {ECO:0000303|PubMed:19043200};
Short=PKS-B;
EC=2.3.1.- {ECO:0000305|PubMed:19043200};
AltName: Full=Hydroxyalkyl alpha-pyrone synthase PKS-B {ECO:0000303|PubMed:21193570};
AltName: Full=Protein LESS ADHESIVE POLLEN 5 {ECO:0000303|PubMed:20442277};
Name=PKSB {ECO:0000303|PubMed:19043200};
Synonyms=LAP5 {ECO:0000312|EMBL:AEE86428.1};
OrderedLocusNames=At4g34850 {ECO:0000312|Araport:AT4G34850};
ORFNames=T11I11.90 {ECO:0000312|EMBL:CAB45446.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702 {ECO:0000312|Proteomes:UP000006548};
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Ag-0, cv. Ba-1, cv. Bl-1, cv. Bla-1, cv. Br-0, cv. Can-0,
cv. Chi-0, cv. Co-1, cv. En-D, cv. En-T, cv. Es-0, cv. Gr-1,
cv. Ita-0, cv. Kin-0, cv. Lip-0, cv. Mt-0, cv. Mv-0, cv. Pog-0,
cv. Ri-0, cv. Rs-1, cv. St-0, cv. Tsu-0, cv. Van-0, and cv. Yo-0;
PubMed=17611127; DOI=10.1016/j.ympev.2007.05.006;
Wang W.-K., Schaal B.A., Chiou Y.-M., Murakami N., Ge X.-J.,
Huang C.-C., Chiang T.-Y.;
"Diverse selective modes among orthologs/paralogs of the chalcone
synthase (Chs) gene family of Arabidopsis thaliana and its relative A.
halleri ssp. gemmifera.";
Mol. Phylogenet. Evol. 44:503-520(2007).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
"Simultaneous high-throughput recombinational cloning of open reading
frames in closed and open configurations.";
Plant Biotechnol. J. 4:317-324(2006).
[6]
FUNCTION, NOMENCLATURE, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=19043200; DOI=10.1248/bpb.31.2205;
Mizuuchi Y., Shimokawa Y., Wanibuchi K., Noguchi H., Abe I.;
"Structure function analysis of novel type III polyketide synthases
from Arabidopsis thaliana.";
Biol. Pharm. Bull. 31:2205-2210(2008).
[7]
FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, TISSUE
SPECIFICITY, AND SUBCELLULAR LOCATION.
STRAIN=cv. Columbia;
PubMed=21193570; DOI=10.1105/tpc.110.080028;
Kim S.S., Grienenberger E., Lallemand B., Colpitts C.C., Kim S.Y.,
de Azevedo Souza C., Geoffroy P., Heintz D., Krahn D., Kaiser M.,
Kombrink E., Heitz T., Suh D.-Y., Legrand M., Douglas C.J.;
"LAP6/POLYKETIDE SYNTHASE A and LAP5/POLYKETIDE SYNTHASE B encode
hydroxyalkyl alpha-pyrone synthases required for pollen development
and sporopollenin biosynthesis in Arabidopsis thaliana.";
Plant Cell 22:4045-4066(2010).
[8]
FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-227, TISSUE
SPECIFICITY, DEVELOPMENTAL STAGE, AND GENE FAMILY.
STRAIN=cv. Landsberg erecta;
PubMed=20442277; DOI=10.1104/pp.110.157446;
Dobritsa A.A., Lei Z., Nishikawa S., Urbanczyk-Wochniak E.,
Huhman D.V., Preuss D., Sumner L.W.;
"LAP5 and LAP6 encode anther-specific proteins with similarity to
chalcone synthase essential for pollen exine development in
Arabidopsis.";
Plant Physiol. 153:937-955(2010).
[9]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH
4CLL1/ACOS5 AND TKPR1.
PubMed=23632852; DOI=10.1104/pp.112.213124;
Lallemand B., Erhardt M., Heitz T., Legrand M.;
"Sporopollenin biosynthetic enzymes interact and constitute a
metabolon localized to the endoplasmic reticulum of tapetum cells.";
Plant Physiol. 162:616-625(2013).
-!- FUNCTION: Plant type III polyketide synthases (PKSs) that
catalyzes the condensation of malonyl-CoA units with various CoA
ester starter molecules to generate a diverse array of natural
products including long-chain alkyl alpha-pyrones. Accepts up to
C(20) chain-length fatty acyl CoAs as starter substrates, and
carries out sequential condensations with malonyl-CoA to produce
triketide and tetraketide alpha-pyrones, potential sporopollenin
precursors (PubMed:19043200, PubMed:21193570). Favorite substrates
for are midchain- and v-hydroxylated fatty acyl-CoAs (e.g. 12-
hydroxyoctadecanoyl-CoA and 16-hydroxyhexadecanoyl-CoA). Required
for pollen development and sporopollenin biosynthesis, the major
constituent of exine in the outer pollen wall (PubMed:21193570,
PubMed:20442277). In vitro, can use 4-coumaroyl-coenzyme A as
substrate to produce bis-noryangonin and fatty acyl-coenzyme A as
substrate to produce medium-chain alkyl pyrones. May play a role
in both the synthesis of pollen fatty acids and phenolics found in
exine (PubMed:20442277). {ECO:0000269|PubMed:19043200,
ECO:0000269|PubMed:20442277, ECO:0000269|PubMed:21193570}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=30.4 uM for n-dodecanoyl-CoA (at pH 7 and 30 degrees Celsius)
{ECO:0000269|PubMed:19043200};
Note=kcat is 0.06 min(-1) with n-dodecanoyl-CoA as substrate for
the production of the triketide alpha-pyrone (at pH 7 and 30
degrees Celsius). {ECO:0000269|PubMed:19043200};
pH dependence:
Optimum pH is 7 (at 30 degrees Celsius).
{ECO:0000269|PubMed:19043200};
-!- PATHWAY: Secondary metabolite biosynthesis; flavonoid
biosynthesis. {ECO:0000250|UniProtKB:Q9LKP7}.
-!- SUBUNIT: Homodimer (By similarity). Interacts with 4CLL1/ACOS5 and
TKPR1 (PubMed:23632852). {ECO:0000250|UniProtKB:P30074,
ECO:0000269|PubMed:23632852}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum
{ECO:0000269|PubMed:21193570, ECO:0000269|PubMed:23632852}.
-!- TISSUE SPECIFICITY: Expressed in flowers and flower buds (at
protein level) (PubMed:21193570, PubMed:20442277). Mostly confined
to anther tapetal cells (PubMed:23632852).
{ECO:0000269|PubMed:20442277, ECO:0000269|PubMed:21193570,
ECO:0000269|PubMed:23632852}.
-!- DEVELOPMENTAL STAGE: Most abundant in the youngest flower buds,
but levels decline as flowers mature. Specifically and transiently
expressed in tapetal cells during microspore development in
anthers (at protein level). {ECO:0000269|PubMed:20442277,
ECO:0000269|PubMed:21193570}.
-!- DISRUPTION PHENOTYPE: Pollen exine layer defects. Reduced
accumulation of flavonoid precursors and flavonoids in developing
anthers. Plants lacking both PKS-A and PKS-B are completely male
sterile, with no apparent exine, thus leading to pollen grain
collapse under vacuum. Altered pollen-stigma adhesion.
{ECO:0000269|PubMed:20442277, ECO:0000269|PubMed:21193570}.
-!- SIMILARITY: Belongs to the chalcone/stilbene synthases family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=ABK28665.1; Type=Erroneous termination; Positions=393; Note=Translated as stop.; Evidence={ECO:0000305};
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EMBL; DQ062353; AAZ23694.1; -; mRNA.
EMBL; DQ062354; AAZ23695.1; -; mRNA.
EMBL; DQ062355; AAZ23696.1; -; mRNA.
EMBL; DQ062356; AAZ23697.1; -; mRNA.
EMBL; DQ062357; AAZ23698.1; -; mRNA.
EMBL; DQ062359; AAZ23700.1; -; mRNA.
EMBL; DQ062360; AAZ23701.1; -; mRNA.
EMBL; DQ062362; AAZ23703.1; -; mRNA.
EMBL; DQ062365; AAZ23706.1; -; mRNA.
EMBL; DQ062366; AAZ23707.1; -; mRNA.
EMBL; DQ062369; AAZ23710.1; -; mRNA.
EMBL; DQ062370; AAZ23711.1; -; mRNA.
EMBL; DQ062371; AAZ23712.1; -; mRNA.
EMBL; DQ062372; AAZ23713.1; -; mRNA.
EMBL; DQ062373; AAZ23714.1; -; mRNA.
EMBL; DQ062374; AAZ23715.1; -; mRNA.
EMBL; DQ062375; AAZ23716.1; -; mRNA.
EMBL; DQ062377; AAZ23718.1; -; mRNA.
EMBL; DQ062378; AAZ23719.1; -; mRNA.
EMBL; DQ062379; AAZ23720.1; -; mRNA.
EMBL; DQ062381; AAZ23722.1; -; mRNA.
EMBL; DQ062382; AAZ23723.1; -; mRNA.
EMBL; DQ062383; AAZ23724.1; -; mRNA.
EMBL; DQ062384; AAZ23725.1; -; mRNA.
EMBL; AL079347; CAB45446.1; -; Genomic_DNA.
EMBL; AL161586; CAB80202.1; -; Genomic_DNA.
EMBL; CP002687; AEE86428.1; -; Genomic_DNA.
EMBL; DQ446894; ABE66111.1; -; mRNA.
EMBL; DQ653244; ABK28665.1; ALT_SEQ; mRNA.
EMBL; AY085918; AAM63130.1; -; mRNA.
PIR; T10231; T10231.
RefSeq; NP_567971.1; NM_119651.4.
UniGene; At.3503; -.
UniGene; At.69687; -.
ProteinModelPortal; Q8LDM2; -.
SMR; Q8LDM2; -.
STRING; 3702.AT4G34850.1; -.
PaxDb; Q8LDM2; -.
EnsemblPlants; AT4G34850.1; AT4G34850.1; AT4G34850.
GeneID; 829637; -.
Gramene; AT4G34850.1; AT4G34850.1; AT4G34850.
KEGG; ath:AT4G34850; -.
Araport; AT4G34850; -.
TAIR; locus:2116845; AT4G34850.
eggNOG; ENOG410IIN2; Eukaryota.
eggNOG; COG3424; LUCA.
HOGENOM; HOG000245460; -.
OMA; CVRSWGG; -.
OrthoDB; EOG09360C3D; -.
PhylomeDB; Q8LDM2; -.
BioCyc; ARA:AT4G34850-MONOMER; -.
BioCyc; MetaCyc:AT4G34850-MONOMER; -.
UniPathway; UPA00154; -.
PRO; PR:Q8LDM2; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q8LDM2; baseline and differential.
Genevisible; Q8LDM2; AT.
GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
GO; GO:0090439; F:tetraketide alpha-pyrone synthase activity; IDA:TAIR.
GO; GO:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0010584; P:pollen exine formation; IMP:TAIR.
GO; GO:0030639; P:polyketide biosynthetic process; IDA:TAIR.
GO; GO:0080110; P:sporopollenin biosynthetic process; IMP:TAIR.
Gene3D; 3.40.47.10; -; 2.
InterPro; IPR012328; Chalcone/stilbene_synth_C.
InterPro; IPR001099; Chalcone/stilbene_synthase_N.
InterPro; IPR011141; Polyketide_synthase_type-III.
InterPro; IPR016039; Thiolase-like.
PANTHER; PTHR11877; PTHR11877; 1.
Pfam; PF02797; Chal_sti_synt_C; 1.
Pfam; PF00195; Chal_sti_synt_N; 1.
PIRSF; PIRSF000451; PKS_III; 1.
SUPFAM; SSF53901; SSF53901; 2.
1: Evidence at protein level;
Acyltransferase; Complete proteome; Developmental protein;
Endoplasmic reticulum; Flavonoid biosynthesis; Reference proteome;
Transferase.
CHAIN 1 392 Type III polyketide synthase B.
/FTId=PRO_0000432841.
REGION 57 64 Coenzyme A binding.
{ECO:0000250|UniProtKB:P30074}.
REGION 218 219 Substrate binding.
{ECO:0000250|UniProtKB:P30074}.
REGION 309 312 Coenzyme A binding.
{ECO:0000250|UniProtKB:Q58VP7}.
ACT_SITE 166 166 Nucleophile.
{ECO:0000250|UniProtKB:Q94FV7,
ECO:0000255|PROSITE-ProRule:PRU10023}.
BINDING 269 269 Coenzyme A; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q58VP7}.
BINDING 312 312 Coenzyme A; via amide nitrogen.
{ECO:0000250|UniProtKB:P30074}.
MUTAGEN 227 227 G->E: In lap5-1; pollen exine layer
defects leading to altered pollen-stigma
adhesion. {ECO:0000269|PubMed:20442277}.
CONFLICT 61 62 Missing (in Ref. 2; CAB45446/CAB80202).
{ECO:0000305}.
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


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