PULA1_ARATH
ID PULA1_ARATH Reviewed; 965 AA.
AC Q8GTR4;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Pullulanase 1, chloroplastic;
DE Short=AtPU1;
DE EC=3.2.1.142;
DE AltName: Full=Protein LIMIT DEXTRINASE;
DE Short=AtLDA;
DE Flags: Precursor;
GN Name=PU1; Synonyms=LDA; OrderedLocusNames=At5g04360; ORFNames=T19N18.90;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=15849301; DOI=10.1104/pp.105.059295;
RA Wattebled F., Dong Y., Dumez S., Delvalle D., Planchot V., Berbezy P.,
RA Vyas D., Colonna P., Chatterjee M., Ball S., D'Hulst C.;
RT "Mutants of Arabidopsis lacking a chloroplastic isoamylase accumulate
RT phytoglycogen and an abnormal form of amylopectin.";
RL Plant Physiol. 138:184-195(2005).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16495218; DOI=10.1074/jbc.m513661200;
RA Delatte T., Umhang M., Trevisan M., Eicke S., Thorneycroft D., Smith S.M.,
RA Zeeman S.C.;
RT "Evidence for distinct mechanisms of starch granule breakdown in plants.";
RL J. Biol. Chem. 281:12050-12059(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
RN [7]
RP FUNCTION.
RX PubMed=19074683; DOI=10.1105/tpc.108.063487;
RA Streb S., Delatte T., Umhang M., Eicke S., Schorderet M., Reinhardt D.,
RA Zeeman S.C.;
RT "Starch granule biosynthesis in Arabidopsis is abolished by removal of all
RT debranching enzymes but restored by the subsequent removal of an
RT endoamylase.";
RL Plant Cell 20:3448-3466(2008).
RN [8]
RP FUNCTION.
RX PubMed=18815382; DOI=10.1104/pp.108.129379;
RA Wattebled F., Planchot V., Dong Y., Szydlowski N., Pontoire B., Devin A.,
RA Ball S., D'Hulst C.;
RT "Further evidence for the mandatory nature of polysaccharide debranching
RT for the aggregation of semicrystalline starch and for overlapping functions
RT of debranching enzymes in Arabidopsis leaves.";
RL Plant Physiol. 148:1309-1323(2008).
CC -!- FUNCTION: Involved in starch degradation and also probably in the
CC trimming of pre-amylopectin chains during starch synthesis.
CC {ECO:0000269|PubMed:16495218, ECO:0000269|PubMed:18815382,
CC ECO:0000269|PubMed:19074683}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic linkages in alpha- and
CC beta-limit dextrins of amylopectin and glycogen, and in amylopectin
CC and pullulan.; EC=3.2.1.142;
CC -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC -!- PATHWAY: Glycan degradation; starch degradation.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:16495218, ECO:0000269|PubMed:18431481}.
CC -!- DISRUPTION PHENOTYPE: No effect on the starch level in leaves and
CC slight increase of water-soluble polysaccharides. No alteration of the
CC amylase-to-amylopectin ratio. ISA3 is able to fully compensate for the
CC loss of PU1. {ECO:0000269|PubMed:15849301}.
CC -!- MISCELLANEOUS: Double mutant shows that PU1 and ISA3 have redundant
CC function for starch degradation. The involvement of PU1 in amylopectin
CC synthesis is infered from the phenotype of double mutant in PU1 and
CC ISA2.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; CP002688; AED90732.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68325.1; -; Genomic_DNA.
DR EMBL; BT002411; AAO00771.1; -; mRNA.
DR RefSeq; NP_001330089.1; NM_001342767.1.
DR RefSeq; NP_196056.2; NM_120518.5.
DR AlphaFoldDB; Q8GTR4; -.
DR SMR; Q8GTR4; -.
DR STRING; 3702.AT5G04360.1; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR MetOSite; Q8GTR4; -.
DR PaxDb; Q8GTR4; -.
DR PRIDE; Q8GTR4; -.
DR ProteomicsDB; 226080; -.
DR EnsemblPlants; AT5G04360.1; AT5G04360.1; AT5G04360.
DR EnsemblPlants; AT5G04360.2; AT5G04360.2; AT5G04360.
DR GeneID; 830315; -.
DR Gramene; AT5G04360.1; AT5G04360.1; AT5G04360.
DR Gramene; AT5G04360.2; AT5G04360.2; AT5G04360.
DR KEGG; ath:AT5G04360; -.
DR Araport; AT5G04360; -.
DR TAIR; locus:2179919; AT5G04360.
DR eggNOG; KOG0470; Eukaryota.
DR HOGENOM; CLU_004744_5_1_1; -.
DR InParanoid; Q8GTR4; -.
DR OMA; DKIVPWY; -.
DR OrthoDB; 533388at2759; -.
DR BioCyc; ARA:AT5G04360-MON; -.
DR UniPathway; UPA00152; -.
DR UniPathway; UPA00153; -.
DR PRO; PR:Q8GTR4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8GTR4; baseline and differential.
DR Genevisible; Q8GTR4; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0010303; F:limit dextrinase activity; IDA:TAIR.
DR GO; GO:0051060; F:pullulanase activity; IDA:TAIR.
DR GO; GO:0019252; P:starch biosynthetic process; IMP:TAIR.
DR GO; GO:0005983; P:starch catabolic process; IMP:TAIR.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR004193; Glyco_hydro_13_N.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR011839; Pullul_strch.
DR InterPro; IPR024561; Pullul_strch_C.
DR InterPro; IPR040671; Pullulanase_N2.
DR InterPro; IPR045041; Pullulanase_PULA-like.
DR PANTHER; PTHR43631; PTHR43631; 1.
DR Pfam; PF02922; CBM_48; 1.
DR Pfam; PF11852; DUF3372; 1.
DR Pfam; PF17967; Pullulanase_N2; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 2.
DR TIGRFAMs; TIGR02103; pullul_strch; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Chloroplast; Glycosidase; Hydrolase; Plastid;
KW Reference proteome; Starch biosynthesis; Transit peptide.
FT TRANSIT 1..62
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 63..965
FT /note="Pullulanase 1, chloroplastic"
FT /id="PRO_0000379530"
FT ACT_SITE 552
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 589
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT SITE 721
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CONFLICT 859
FT /note="Q -> K (in Ref. 3; AAO00771)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 965 AA; 107067 MW; 27074C8B5D71BDAC CRC64;
MALTLTPTSS VHLLSSISVA RPRIFAADFN LRSRWRRRRP VTSISNFRLR LPSKTSLHCL
CSSSSASSPM SLEVSSPNSQ FLDCLIYSRA YWVTQGVIAW NVDVGEGSCY FYASKSAGLS
FSEDGIDGYD LRIKLEAESG SLPADVIEKF PHIRNYKSFK VPKDLDIRDL VKSQLAVVCF
DAEGRLIQGT GLQLPGVLDE LFSYDGPLGA HFTPEGVSLH LWAPTAQAVS VCIYKNPLDK
SPMEICPLKE ANGVWSTEGA CSWGGCYYVY KVSVYHPSTM KLETCYANDP YARGLSADGR
KTFLVNLDSD DLKPEGWDNL ADKKPCLRSF SDISIYELHV RDFSANDETV EPENRGGYLA
FTSKDSAGVK HLQKLVDAGL THLHLLPTFQ FGDVDDEKEN WKSVDTSLLE GLRPDSTEAQ
ARITEIQNDD GYNWGYNPVL WGVPKGSYAS DPTGPCRIIE FRKMVQALNC TGLNVVLDVV
YNHLHASGPH DKESVLDKIV PGYYLRRNSD GFIENSTCVN NTASEHYMVD RLIRDDLLNW
VVNYKVDGFR FDLMGHIMKA TIVNAKSAIG SLRKETDGVD GSRIYLYGEG WNFGEVAENG
RGINASQFNL GGTGIGSFND RIRDATLGGS PFGHPLQQGF ITGLLLQPNA HDHGSEATQE
LMLSTAKNHI QTGMAANLKD YMLTNHEGKE VKGSEVLMHD ATPVAYASLP TETINYVSAH
DNETLFDIIS LKTPMEISVD ERCRINHLAS SMIALSQGIP FFHAGDEILR SKSLDRDSYN
SGDWFNRLDF SYSSNNWGVG LPPKGKNEHN WPLIKPRLQD PSFKPKSSHI VATLHNFLDL
LRIRYSSPLF RLDTARAIQE RVRFHNTGPS SIPGAIVMSI EDGHRGIPSV SQIDPIYSLI
VVIFNARPSE FSYPSPALKD RKLELHPVQV MSADEIVKKS VYDSFSGGFT VPARTTTVFV
ESRNG
