ISOA1_ARATH
ID ISOA1_ARATH Reviewed; 783 AA.
AC O04196;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Isoamylase 1, chloroplastic;
DE Short=AtISA1;
DE EC=3.2.1.68;
DE Flags: Precursor;
GN Name=ISA1; OrderedLocusNames=At2g39930; ORFNames=T28M21.9;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 ISA2, 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 ISA2, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in
CC glycogen, amylopectin and their beta-limit dextrins.; EC=3.2.1.68;
CC -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC -!- SUBUNIT: Associates with ISA2 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 -!- MISCELLANEOUS: In the absence of ISA2, ISA1 may be unstable.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; AF002109; AAB95278.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09752.1; -; Genomic_DNA.
DR EMBL; BT000443; AAN17420.1; -; mRNA.
DR EMBL; BT010348; AAQ56791.1; -; mRNA.
DR PIR; B84823; B84823.
DR RefSeq; NP_181522.1; NM_129551.4.
DR AlphaFoldDB; O04196; -.
DR SMR; O04196; -.
DR BioGRID; 3918; 2.
DR IntAct; O04196; 2.
DR STRING; 3702.AT2G39930.1; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PaxDb; O04196; -.
DR PRIDE; O04196; -.
DR ProteomicsDB; 232228; -.
DR EnsemblPlants; AT2G39930.1; AT2G39930.1; AT2G39930.
DR GeneID; 818580; -.
DR Gramene; AT2G39930.1; AT2G39930.1; AT2G39930.
DR KEGG; ath:AT2G39930; -.
DR Araport; AT2G39930; -.
DR TAIR; locus:2061216; AT2G39930.
DR eggNOG; KOG0470; Eukaryota.
DR HOGENOM; CLU_011725_1_1_1; -.
DR InParanoid; O04196; -.
DR OrthoDB; 533388at2759; -.
DR PhylomeDB; O04196; -.
DR BioCyc; ARA:AT2G39930-MON; -.
DR BRENDA; 3.2.1.68; 399.
DR UniPathway; UPA00152; -.
DR PRO; PR:O04196; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O04196; baseline and differential.
DR Genevisible; O04196; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0010368; C:chloroplast isoamylase complex; IDA: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 GO; GO:0005983; P:starch catabolic process; IEA:EnsemblPlants.
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; 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; Glycosidase; Hydrolase; Plastid;
KW Reference proteome; Starch biosynthesis; Transit peptide.
FT TRANSIT 1..43
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 44..783
FT /note="Isoamylase 1, chloroplastic"
FT /id="PRO_0000379527"
FT ACT_SITE 410
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT ACT_SITE 466
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT SITE 538
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P04746"
SQ SEQUENCE 783 AA; 89481 MW; 638A6F9088CDB896 CRC64;
MDAIKCSSSF LHHTKLNTLF SNHTFPKISA PNFKPLFRPI SISAKDRRSN EAENIAVVEK
PLKSDRFFIS DGLPSPFGPT VRDDGVNFSV YSTNSVSATI CLISLSDLRQ NKVTEEIQLD
PSRNRTGHVW HVFLRGDFKD MLYGYRFDGK FSPEEGHYYD SSNILLDPYA KAIISRDEFG
VLGPDDNCWP QMACMVPTRE EEFDWEGDMH LKLPQKDLVI YEMHVRGFTR HESSKIEFPG
TYQGVAEKLD HLKELGINCI ELMPCHEFNE LEYYSYNTIL GDHRVNFWGY STIGFFSPMI
RYASASSNNF AGRAINEFKI LVKEAHKRGI EVIMDVVLNH TAEGNEKGPI FSFRGVDNSV
YYMLAPKGEF YNYSGCGNTF NCNHPVVRQF ILDCLRYWVT EMHVDGFRFD LGSIMSRSSS
LWDAANVYGA DVEGDLLTTG TPISCPPVID MISNDPILRG VKLIAEAWDA GGLYQVGMFP
HWGIWSEWNG KFRDVVRQFI KGTDGFSGAF AECLCGSPNL YQGGRKPWHS INFICAHDGF
TLADLVTYNN KNNLANGEEN NDGENHNYSW NCGEEGDFAS ISVKRLRKRQ MRNFFVSLMV
SQGVPMIYMG DEYGHTKGGN NNTYCHDNYM NYFRWDKKEE AHSDFFRFCR ILIKFRDECE
SLGLNDFPTA KRLQWHGLAP EIPNWSETSR FVAFSLVDSV KKEIYVAFNT SHLATLVSLP
NRPGYRWEPF VDTSKPSPYD CITPDLPERE TAMKQYRHFL DANVYPMLSY SSIILLLSPI
KDP
