ISOA2_ARATH
ID ISOA2_ARATH Reviewed; 882 AA.
AC Q8L735; Q9ZVT2;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Isoamylase 2, chloroplastic;
DE Short=AtISA2;
DE AltName: Full=Protein DEBRANCHING ENZYME 1;
DE Flags: Precursor;
GN Name=ISA2; Synonyms=DBE1; OrderedLocusNames=At1g03310; ORFNames=F15K9.9;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 FUNCTION, INTERACTION WITH ISA1, AND DISRUPTION PHENOTYPE.
RX PubMed=15743447; DOI=10.1111/j.1365-313x.2005.02348.x;
RA Delatte T., Trevisan M., Parker M.L., Zeeman S.C.;
RT "Arabidopsis mutants Atisa1 and Atisa2 have identical phenotypes and lack
RT the same multimeric isoamylase, which influences the branch point
RT distribution of amylopectin during starch synthesis.";
RL Plant J. 41:815-830(2005).
RN [5]
RP INTERACTION WITH ISA1, AND 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 [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 the trimming of pre-amylopectin chains.
CC Accelerates the crystallization of nascent amylopectin molecules during
CC starch synthesis. ISA1 and ISA2 work exclusively together as a
CC multimeric holoenzyme. ISA1-ISA2 removes preferentially branches that
CC are very close to other branches. {ECO:0000269|PubMed:15743447,
CC ECO:0000269|PubMed:18815382, ECO:0000269|PubMed:19074683}.
CC -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC -!- SUBUNIT: Associates with ISA1 to form the heteromultimeric complex Iso1
CC required for amylopectin synthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:18431481}.
CC -!- DISRUPTION PHENOTYPE: Strong reduction of the starch level in leaves,
CC but 50-fold increase of water-soluble polysaccharides. No alteration of
CC the amylase-to-amylopectin ratio. {ECO:0000269|PubMed:15743447,
CC ECO:0000269|PubMed:15849301}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
CC -!- CAUTION: Amino acids thought to be required for catalysis are not
CC conserved in ISA2, suggesting that it may not be an active debranching
CC enzyme and acts via its interaction with ISA1. {ECO:0000305}.
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DR EMBL; AC005278; AAC72113.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27557.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27558.1; -; Genomic_DNA.
DR EMBL; AY139980; AAM98123.1; -; mRNA.
DR PIR; F86164; F86164.
DR RefSeq; NP_171830.1; NM_100213.4.
DR RefSeq; NP_973751.1; NM_202022.3.
DR AlphaFoldDB; Q8L735; -.
DR SMR; Q8L735; -.
DR STRING; 3702.AT1G03310.2; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PaxDb; Q8L735; -.
DR PRIDE; Q8L735; -.
DR ProteomicsDB; 228835; -.
DR EnsemblPlants; AT1G03310.1; AT1G03310.1; AT1G03310.
DR EnsemblPlants; AT1G03310.2; AT1G03310.2; AT1G03310.
DR GeneID; 839531; -.
DR Gramene; AT1G03310.1; AT1G03310.1; AT1G03310.
DR Gramene; AT1G03310.2; AT1G03310.2; AT1G03310.
DR KEGG; ath:AT1G03310; -.
DR Araport; AT1G03310; -.
DR TAIR; locus:2014500; AT1G03310.
DR eggNOG; KOG0470; Eukaryota.
DR HOGENOM; CLU_011725_2_0_1; -.
DR InParanoid; Q8L735; -.
DR OMA; EPIFPFD; -.
DR OrthoDB; 533388at2759; -.
DR PhylomeDB; Q8L735; -.
DR BioCyc; ARA:AT1G03310-MON; -.
DR BioCyc; MetaCyc:AT1G03310-MON; -.
DR BRENDA; 3.2.1.68; 399.
DR UniPathway; UPA00152; -.
DR PRO; PR:Q8L735; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8L735; baseline and differential.
DR Genevisible; Q8L735; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0019156; F:isoamylase activity; IDA:TAIR.
DR GO; GO:0010021; P:amylopectin biosynthetic process; IMP:TAIR.
DR GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd11346; AmyAc_plant_IsoA; 1.
DR CDD; cd02856; E_set_GDE_Isoamylase_N; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR044096; AmyAc_plant_ISA2.
DR InterPro; IPR044505; GlgX_Isoamylase_N_E_set.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
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 Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02922; CBM_48; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Chloroplast; Plastid; Reference proteome;
KW Starch biosynthesis; Transit peptide.
FT TRANSIT 1..70
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 71..882
FT /note="Isoamylase 2, chloroplastic"
FT /id="PRO_0000379528"
FT CONFLICT 211
FT /note="Q -> R (in Ref. 3; AAM98123)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 882 AA; 98884 MW; 277940176F03B06D CRC64;
MAAWSPSVGI GSCCLNNGIT RTWKFPSARL FTGRKNKIKL GSETLMFTRK RFMGDLVTSA
LQSYQFSKIC ASKTSIELRE ALSSRRAEAD DLKKVTSYSF RTKAGALVKV KVEKKREKYS
ILVYVSSLEL SGDDKSRLVM VWGVYRSDSS CFLPLDFENS SQDSQTHTTE TTFVKSSLSE
LMLGLEFDGK ESPFYLSFHL KLVSGRDPDG QEMLTHRDTD FCIPVGFTAG HPLPLGLSSG
PDDDSWNFSF FSRSSTNVVL CLYDDSTTDK PALELDLDPY VNRTGDVWHA SVDNTWDFVR
YGYRCKETAH SKEDVDVEGE PIVLDPYATV VGKSVSQKYL GSLSKSPSFD WGEDVSPNIP
LEKLLVYRLN VKGFTQHRSS KLPSNVAGTF SGVAEKVSHL KTLGTNAVLL EPIFSFSEQK
GPYFPFHFFS PMDIYGPSNS LESAVNSMKV MVKKLHSEGI EVLLEVVFTH TADSGALRGI
DDSSYYYKGR ANDLDSKSYL NCNYPVVQQL VLESLRYWVT EFHVDGFCFI NASSLLRGVH
GEQLSRPPLV EAIAFDPLLA ETKLIADCWD PLEMMPKEVR FPHWKRWAEL NTRYCRNVRN
FLRGRGVLSD LATRICGSGD VFTDGRGPAF SFNYISRNSG LSLVDIVSFS GPELASELSW
NCGEEGATNK SAVLQRRLKQ IRNFLFIQYI SLGVPVLNMG DECGISTRGS PLLESRKPFD
WNLLASAFGT QITQFISFMT SVRARRSDVF QRRDFLKPEN IVWYANDQTT PKWEDPASKF
LALEIKSESE EEETASLAEP NEPKSNDLFI GFNASDHPES VVLPSLPDGS KWRRLVDTAL
PFPGFFSVEG ETVVAEEPLQ QLVVYEMKPY SCTLFETINT TA
