Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Isoamylase 3, chloroplastic

Gene

ISA3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Involved in starch catabolism. ISA3 removes different branches than ISA1-ISA2, namely short chains that prevent amylopectin crystallization. May be the debranching enzyme required to assist beta-amylases for starch degradation in leaves at night.3 Publications

Catalytic activityi

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

Pathwayi: starch degradation

This protein is involved in the pathway starch degradation, which is part of Glycan degradation.
View all proteins of this organism that are known to be involved in the pathway starch degradation and in Glycan degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei428 – 4281NucleophileBy similarity
Active sitei465 – 4651Proton donorBy similarity
Sitei538 – 5381Transition state stabilizerBy similarity

GO - Molecular functioni

  • isoamylase activity Source: TAIR

GO - Biological processi

  • glycogen metabolic process Source: GOC
  • starch catabolic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

BioCyciARA:AT4G09020-MONOMER.
MetaCyc:AT4G09020-MONOMER.
BRENDAi3.2.1.68. 399.
UniPathwayiUPA00153.

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Isoamylase 3, chloroplastic (EC:3.2.1.68)
Short name:
AtISA3
Gene namesi
Name:ISA3
Ordered Locus Names:At4g09020
ORF Names:F23J3.50
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G09020.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast starch grain Source: TAIR
  • chloroplast stroma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Disruption phenotypei

Strong increase of the starch level in leaves at the end of both day and night periods, but no modification in water-soluble polysaccharides content. No alteration of the amylase-to-amylopectin ratio.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 7070ChloroplastSequence analysisAdd
BLAST
Chaini71 – 764694Isoamylase 3, chloroplasticPRO_0000379529Add
BLAST

Proteomic databases

PaxDbiQ9M0S5.
PRIDEiQ9M0S5.

PTM databases

iPTMnetiQ9M0S5.

Expressioni

Gene expression databases

GenevisibleiQ9M0S5. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G09020.1.

Structurei

3D structure databases

ProteinModelPortaliQ9M0S5.
SMRiQ9M0S5. Positions 87-763.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IN7N. Eukaryota.
COG1523. LUCA.
HOGENOMiHOG000239197.
InParanoidiQ9M0S5.
KOiK01214.
OMAiGETNDLN.
PhylomeDBiQ9M0S5.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004193. Glyco_hydro_13_N.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02922. CBM_48. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
SSF81296. SSF81296. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9M0S5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTSPSSSST YDPFSSNFSP SLTNAFSSSF TIPMGLKLSR RVTRARIFSR
60 70 80 90 100
KIKDRSTLKV TCRRAHERVV EEEASTMTET KLFKVSSGEV SPLGVSQVDK
110 120 130 140 150
GINFALFSQN ATSVTLCLSL SQSGKDDTDD DGMIELVLDP SVNKTGDTWH
160 170 180 190 200
ICVEDLPLNN VLYGYRVDGP GEWQQGHRFD RSILLLDPYA KLVKGHSSFG
210 220 230 240 250
DSSQKFAQFY GTYDFESSPF DWGDDYKFPN IPEKDLVIYE MNVRAFTADE
260 270 280 290 300
SSGMDPAIGG SYLGFIEKIP HLQDLGINAV ELLPVFEFDE LELQRRSNPR
310 320 330 340 350
DHMVNTWGYS TVNFFAPMSR YASGEGDPIK ASKEFKEMVK ALHSAGIEVI
360 370 380 390 400
LDVVYNHTNE ADDKYPYTTS FRGIDNKVYY MLDPNNQLLN FSGCGNTLNC
410 420 430 440 450
NHPVVMELIL DSLRHWVTEY HVDGFRFDLA SVLCRATDGS PLSAPPLIRA
460 470 480 490 500
IAKDSVLSRC KIIAEPWDCG GLYLVGKFPN WDRWAEWNGM YRDDVRRFIK
510 520 530 540 550
GDSGMKGSFA TRVSGSSDLY QVNQRKPYHG VNFVIAHDGF TLRDLVSYNF
560 570 580 590 600
KHNEANGEGG NDGCNDNHSW NCGFEGETGD AHIKSLRTRQ MKNFHLALMI
610 620 630 640 650
SQGTPMMLMG DEYGHTRYGN NNSYGHDTSL NNFQWKELDA KKQNHFRFFS
660 670 680 690 700
EVIKFRHSHH VLKHENFLTQ GEITWHEDNW DNSESKFLAF TLHDGIGGRD
710 720 730 740 750
IYVAFNAHDY FVKALIPQPP PGKQWFRVAD TNLESPDDFV REGVAGVADT
760
YNVAPFSSIL LQSK
Length:764
Mass (Da):86,322
Last modified:July 7, 2009 - v2
Checksum:iEE9F163AE7F5E052
GO

Sequence cautioni

The sequence CAB78026.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL161513 Genomic DNA. Translation: CAB78026.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE82713.1.
AY091058 mRNA. Translation: AAM13879.1.
AY133739 mRNA. Translation: AAM91673.1.
AK227049 mRNA. Translation: BAE99109.1.
PIRiB85091.
RefSeqiNP_192641.2. NM_116971.5.
UniGeneiAt.33717.

Genome annotation databases

EnsemblPlantsiAT4G09020.1; AT4G09020.1; AT4G09020.
GeneIDi826481.
GrameneiAT4G09020.1; AT4G09020.1; AT4G09020.
KEGGiath:AT4G09020.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL161513 Genomic DNA. Translation: CAB78026.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE82713.1.
AY091058 mRNA. Translation: AAM13879.1.
AY133739 mRNA. Translation: AAM91673.1.
AK227049 mRNA. Translation: BAE99109.1.
PIRiB85091.
RefSeqiNP_192641.2. NM_116971.5.
UniGeneiAt.33717.

3D structure databases

ProteinModelPortaliQ9M0S5.
SMRiQ9M0S5. Positions 87-763.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G09020.1.

Protein family/group databases

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

PTM databases

iPTMnetiQ9M0S5.

Proteomic databases

PaxDbiQ9M0S5.
PRIDEiQ9M0S5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G09020.1; AT4G09020.1; AT4G09020.
GeneIDi826481.
GrameneiAT4G09020.1; AT4G09020.1; AT4G09020.
KEGGiath:AT4G09020.

Organism-specific databases

TAIRiAT4G09020.

Phylogenomic databases

eggNOGiENOG410IN7N. Eukaryota.
COG1523. LUCA.
HOGENOMiHOG000239197.
InParanoidiQ9M0S5.
KOiK01214.
OMAiGETNDLN.
PhylomeDBiQ9M0S5.

Enzyme and pathway databases

UniPathwayiUPA00153.
BioCyciARA:AT4G09020-MONOMER.
MetaCyc:AT4G09020-MONOMER.
BRENDAi3.2.1.68. 399.

Miscellaneous databases

PROiQ9M0S5.

Gene expression databases

GenevisibleiQ9M0S5. AT.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004193. Glyco_hydro_13_N.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02922. CBM_48. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
SSF81296. SSF81296. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [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. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "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.
  6. "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, DISRUPTION PHENOTYPE.
  7. "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].
  8. "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.
  9. "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 nameiISOA3_ARATH
AccessioniPrimary (citable) accession number: Q9M0S5
Secondary accession number(s): Q8RWW6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 7, 2009
Last sequence update: July 7, 2009
Last modified: May 11, 2016
This is version 100 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 ISA3 and PU1 have redundant function for starch degradation.

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.