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Q8GTR4

- PULA1_ARATH

UniProt

Q8GTR4 - PULA1_ARATH

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Protein
Pullulanase 1, chloroplastic
Gene
PU1, LDA, At5g04360, T19N18.90
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

Involved in starch degradation and also probably in the trimming of pre-amylopectin chains during starch synthesis.3 Publications

Catalytic activityi

Hydrolysis of (1->6)-alpha-D-glucosidic linkages in alpha- and beta-limit dextrins of amylopectin and glycogen, and in amylopectin and pullulan.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei552 – 5521Nucleophile By similarity
Active sitei589 – 5891Proton donor By similarity
Sitei721 – 7211Transition state stabilizer By similarity

GO - Molecular functioni

  1. cation binding Source: InterPro
  2. limit dextrinase activity Source: TAIR
  3. pullulanase activity Source: TAIR

GO - Biological processi

  1. starch biosynthetic process Source: TAIR
  2. starch catabolic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Starch biosynthesis

Enzyme and pathway databases

BioCyciARA:AT5G04360-MONOMER.
UniPathwayiUPA00152.
UPA00153.

Protein family/group databases

CAZyiCBM48. Carbohydrate-Binding Module Family 48.
GH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Pullulanase 1, chloroplastic (EC:3.2.1.142)
Short name:
AtPU1
Alternative name(s):
Protein LIMIT DEXTRINASE
Short name:
AtLDA
Gene namesi
Name:PU1
Synonyms:LDA
Ordered Locus Names:At5g04360
ORF Names:T19N18.90
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 5

Organism-specific databases

TAIRiAT5G04360.

Subcellular locationi

Plastidchloroplast stroma 2 Publications

GO - Cellular componenti

  1. chloroplast Source: TAIR
  2. chloroplast stroma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Disruption phenotypei

No effect on the starch level in leaves and slight increase of water-soluble polysaccharides. No alteration of the amylase-to-amylopectin ratio. ISA3 is able to fully compensate for the loss of PU1.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6262Chloroplast Reviewed prediction
Add
BLAST
Chaini63 – 965903Pullulanase 1, chloroplastic
PRO_0000379530Add
BLAST

Proteomic databases

PaxDbiQ8GTR4.
PRIDEiQ8GTR4.

Expressioni

Gene expression databases

GenevestigatoriQ8GTR4.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT5G04360.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ8GTR4.
SMRiQ8GTR4. Positions 88-963.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi62 – 687Poly-Ser

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1523.
HOGENOMiHOG000251916.
InParanoidiQ8GTR4.
OMAiERCRINH.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.20.20.80. 3 hits.
InterProiIPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004193. Glyco_hydro_13_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR011839. Pullul_strch.
IPR024561. Pullul_strch_C.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02922. CBM_48. 1 hit.
PF11852. DUF3372. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 2 hits.
TIGRFAMsiTIGR02103. pullul_strch. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8GTR4-1 [UniParc]FASTAAdd to Basket

« Hide

MALTLTPTSS VHLLSSISVA RPRIFAADFN LRSRWRRRRP VTSISNFRLR    50
LPSKTSLHCL CSSSSASSPM SLEVSSPNSQ FLDCLIYSRA YWVTQGVIAW 100
NVDVGEGSCY FYASKSAGLS FSEDGIDGYD LRIKLEAESG SLPADVIEKF 150
PHIRNYKSFK VPKDLDIRDL VKSQLAVVCF DAEGRLIQGT GLQLPGVLDE 200
LFSYDGPLGA HFTPEGVSLH LWAPTAQAVS VCIYKNPLDK SPMEICPLKE 250
ANGVWSTEGA CSWGGCYYVY KVSVYHPSTM KLETCYANDP YARGLSADGR 300
KTFLVNLDSD DLKPEGWDNL ADKKPCLRSF SDISIYELHV RDFSANDETV 350
EPENRGGYLA FTSKDSAGVK HLQKLVDAGL THLHLLPTFQ FGDVDDEKEN 400
WKSVDTSLLE GLRPDSTEAQ ARITEIQNDD GYNWGYNPVL WGVPKGSYAS 450
DPTGPCRIIE FRKMVQALNC TGLNVVLDVV YNHLHASGPH DKESVLDKIV 500
PGYYLRRNSD GFIENSTCVN NTASEHYMVD RLIRDDLLNW VVNYKVDGFR 550
FDLMGHIMKA TIVNAKSAIG SLRKETDGVD GSRIYLYGEG WNFGEVAENG 600
RGINASQFNL GGTGIGSFND RIRDATLGGS PFGHPLQQGF ITGLLLQPNA 650
HDHGSEATQE LMLSTAKNHI QTGMAANLKD YMLTNHEGKE VKGSEVLMHD 700
ATPVAYASLP TETINYVSAH DNETLFDIIS LKTPMEISVD ERCRINHLAS 750
SMIALSQGIP FFHAGDEILR SKSLDRDSYN SGDWFNRLDF SYSSNNWGVG 800
LPPKGKNEHN WPLIKPRLQD PSFKPKSSHI VATLHNFLDL LRIRYSSPLF 850
RLDTARAIQE RVRFHNTGPS SIPGAIVMSI EDGHRGIPSV SQIDPIYSLI 900
VVIFNARPSE FSYPSPALKD RKLELHPVQV MSADEIVKKS VYDSFSGGFT 950
VPARTTTVFV ESRNG 965
Length:965
Mass (Da):107,067
Last modified:May 3, 2011 - v2
Checksum:i27074C8B5D71BDAC
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti859 – 8591Q → K in AAO00771. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002688 Genomic DNA. Translation: AED90732.1.
BT002411 mRNA. Translation: AAO00771.1.
RefSeqiNP_196056.2. NM_120518.4.
UniGeneiAt.26109.

Genome annotation databases

EnsemblPlantsiAT5G04360.1; AT5G04360.1; AT5G04360.
GeneIDi830315.
KEGGiath:AT5G04360.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002688 Genomic DNA. Translation: AED90732.1 .
BT002411 mRNA. Translation: AAO00771.1 .
RefSeqi NP_196056.2. NM_120518.4.
UniGenei At.26109.

3D structure databases

ProteinModelPortali Q8GTR4.
SMRi Q8GTR4. Positions 88-963.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 3702.AT5G04360.1-P.

Protein family/group databases

CAZyi CBM48. Carbohydrate-Binding Module Family 48.
GH13. Glycoside Hydrolase Family 13.

Proteomic databases

PaxDbi Q8GTR4.
PRIDEi Q8GTR4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT5G04360.1 ; AT5G04360.1 ; AT5G04360 .
GeneIDi 830315.
KEGGi ath:AT5G04360.

Organism-specific databases

TAIRi AT5G04360.

Phylogenomic databases

eggNOGi COG1523.
HOGENOMi HOG000251916.
InParanoidi Q8GTR4.
OMAi ERCRINH.

Enzyme and pathway databases

UniPathwayi UPA00152 .
UPA00153 .
BioCyci ARA:AT5G04360-MONOMER.

Gene expression databases

Genevestigatori Q8GTR4.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
3.20.20.80. 3 hits.
InterProi IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004193. Glyco_hydro_13_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR011839. Pullul_strch.
IPR024561. Pullul_strch_C.
[Graphical view ]
PANTHERi PTHR10357. PTHR10357. 1 hit.
Pfami PF00128. Alpha-amylase. 1 hit.
PF02922. CBM_48. 1 hit.
PF11852. DUF3372. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 2 hits.
TIGRFAMsi TIGR02103. pullul_strch. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Mutants of Arabidopsis lacking a chloroplastic isoamylase accumulate phytoglycogen and an abnormal form of amylopectin."
    Wattebled F., Dong Y., Dumez S., Delvalle D., Planchot V., Berbezy P., Vyas D., Colonna P., Chatterjee M., Ball S., D'Hulst C.
    Plant Physiol. 138:184-195(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  5. "Evidence for distinct mechanisms of starch granule breakdown in plants."
    Delatte T., Umhang M., Trevisan M., Eicke S., Thorneycroft D., Smith S.M., Zeeman S.C.
    J. Biol. Chem. 281:12050-12059(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  6. "Sorting signals, N-terminal modifications and abundance of the chloroplast proteome."
    Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q., van Wijk K.J.
    PLoS ONE 3:E1994-E1994(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. "Starch granule biosynthesis in Arabidopsis is abolished by removal of all debranching enzymes but restored by the subsequent removal of an endoamylase."
    Streb S., Delatte T., Umhang M., Eicke S., Schorderet M., Reinhardt D., Zeeman S.C.
    Plant Cell 20:3448-3466(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Further evidence for the mandatory nature of polysaccharide debranching for the aggregation of semicrystalline starch and for overlapping functions of debranching enzymes in Arabidopsis leaves."
    Wattebled F., Planchot V., Dong Y., Szydlowski N., Pontoire B., Devin A., Ball S., D'Hulst C.
    Plant Physiol. 148:1309-1323(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiPULA1_ARATH
AccessioniPrimary (citable) accession number: Q8GTR4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 7, 2009
Last sequence update: May 3, 2011
Last modified: April 16, 2014
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Double mutant shows that PU1 and ISA3 have redundant function for starch degradation. The involvement of PU1 in amylopectin synthesis is infered from the phenotype of double mutant in PU1 and ISA2.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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