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Q8GTR4 (PULA1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pullulanase 1, chloroplastic

Short name=AtPU1
EC=3.2.1.142
Alternative name(s):
Protein LIMIT DEXTRINASE
Short name=AtLDA
Gene names
Name:PU1
Synonyms:LDA
Ordered Locus Names:At5g04360
ORF Names:T19N18.90
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length965 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Involved in starch degradation and also probably in the trimming of pre-amylopectin chains during starch synthesis. Ref.5 Ref.7 Ref.8

Catalytic activity

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

Pathway

Glycan biosynthesis; starch biosynthesis.

Glycan degradation; starch degradation.

Subcellular location

Plastidchloroplast stroma Ref.5 Ref.6.

Disruption phenotype

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. Ref.4

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.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6262Chloroplast Potential
Chain63 – 965903Pullulanase 1, chloroplastic
PRO_0000379530

Regions

Compositional bias62 – 687Poly-Ser

Sites

Active site5521Nucleophile By similarity
Active site5891Proton donor By similarity
Site7211Transition state stabilizer By similarity

Experimental info

Sequence conflict8591Q → K in AAO00771. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q8GTR4 [UniParc].

Last modified May 3, 2011. Version 2.
Checksum: 27074C8B5D71BDAC

FASTA965107,067
        10         20         30         40         50         60 
MALTLTPTSS VHLLSSISVA RPRIFAADFN LRSRWRRRRP VTSISNFRLR LPSKTSLHCL 

        70         80         90        100        110        120 
CSSSSASSPM SLEVSSPNSQ FLDCLIYSRA YWVTQGVIAW NVDVGEGSCY FYASKSAGLS 

       130        140        150        160        170        180 
FSEDGIDGYD LRIKLEAESG SLPADVIEKF PHIRNYKSFK VPKDLDIRDL VKSQLAVVCF 

       190        200        210        220        230        240 
DAEGRLIQGT GLQLPGVLDE LFSYDGPLGA HFTPEGVSLH LWAPTAQAVS VCIYKNPLDK 

       250        260        270        280        290        300 
SPMEICPLKE ANGVWSTEGA CSWGGCYYVY KVSVYHPSTM KLETCYANDP YARGLSADGR 

       310        320        330        340        350        360 
KTFLVNLDSD DLKPEGWDNL ADKKPCLRSF SDISIYELHV RDFSANDETV EPENRGGYLA 

       370        380        390        400        410        420 
FTSKDSAGVK HLQKLVDAGL THLHLLPTFQ FGDVDDEKEN WKSVDTSLLE GLRPDSTEAQ 

       430        440        450        460        470        480 
ARITEIQNDD GYNWGYNPVL WGVPKGSYAS DPTGPCRIIE FRKMVQALNC TGLNVVLDVV 

       490        500        510        520        530        540 
YNHLHASGPH DKESVLDKIV PGYYLRRNSD GFIENSTCVN NTASEHYMVD RLIRDDLLNW 

       550        560        570        580        590        600 
VVNYKVDGFR FDLMGHIMKA TIVNAKSAIG SLRKETDGVD GSRIYLYGEG WNFGEVAENG 

       610        620        630        640        650        660 
RGINASQFNL GGTGIGSFND RIRDATLGGS PFGHPLQQGF ITGLLLQPNA HDHGSEATQE 

       670        680        690        700        710        720 
LMLSTAKNHI QTGMAANLKD YMLTNHEGKE VKGSEVLMHD ATPVAYASLP TETINYVSAH 

       730        740        750        760        770        780 
DNETLFDIIS LKTPMEISVD ERCRINHLAS SMIALSQGIP FFHAGDEILR SKSLDRDSYN 

       790        800        810        820        830        840 
SGDWFNRLDF SYSSNNWGVG LPPKGKNEHN WPLIKPRLQD PSFKPKSSHI VATLHNFLDL 

       850        860        870        880        890        900 
LRIRYSSPLF RLDTARAIQE RVRFHNTGPS SIPGAIVMSI EDGHRGIPSV SQIDPIYSLI 

       910        920        930        940        950        960 
VVIFNARPSE FSYPSPALKD RKLELHPVQV MSADEIVKKS VYDSFSGGFT VPARTTTVFV 


ESRNG 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002688 Genomic DNA. Translation: AED90732.1.
BT002411 mRNA. Translation: AAO00771.1.
RefSeqNP_196056.2. NM_120518.4.
UniGeneAt.26109.

3D structure databases

ProteinModelPortalQ8GTR4.
SMRQ8GTR4. Positions 88-963.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT5G04360.1-P.

Protein family/group databases

CAZyCBM48. Carbohydrate-Binding Module Family 48.
GH13. Glycoside Hydrolase Family 13.

Proteomic databases

PaxDbQ8GTR4.
PRIDEQ8GTR4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G04360.1; AT5G04360.1; AT5G04360.
GeneID830315.
KEGGath:AT5G04360.

Organism-specific databases

TAIRAT5G04360.

Phylogenomic databases

eggNOGCOG1523.
HOGENOMHOG000251916.
InParanoidQ8GTR4.
OMAERCRINH.

Enzyme and pathway databases

BioCycARA:AT5G04360-MONOMER.
UniPathwayUPA00152.
UPA00153.

Gene expression databases

GenevestigatorQ8GTR4.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
3.20.20.80. 3 hits.
InterProIPR015902. 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]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF02922. CBM_48. 1 hit.
PF11852. DUF3372. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 2 hits.
TIGRFAMsTIGR02103. pullul_strch. 1 hit.
ProtoNetSearch...

Entry information

Entry namePULA1_ARATH
AccessionPrimary (citable) accession number: Q8GTR4
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names