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TAIR:LDA

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Contents

Species (Taxon ID) Arabidopsis thaliana (thale cress) (taxon:3702)
Gene Name(s) LDA ( synonyms: AT5G04360, ATPU1, ATLDA, PU1, PULLULANASE 1, limit dextrinase, AT5G04360.1, T19N18.90, T19N18_90, PULLULANASE, Limit dextrinase, LDA )
Protein Name(s) limit dextrinase, AT5G04360,
External Links
TAIR locus:2179919

Annotations

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0003824

catalytic activity

TAIR:AnalysisReference:501748310

IEA: Inferred from Electronic Annotation

INTERPRO:IPR006047
INTERPRO:IPR013781

F

From TAIR

GO:0004553

hydrolase activity, hydrolyzing O-glycosyl compounds

TAIR:AnalysisReference:501748310

IEA: Inferred from Electronic Annotation

INTERPRO:IPR004193

F

From TAIR

GO:0004556

alpha-amylase activity

TAIR:Communication:501714663

ISS: Inferred from Sequence or Structural Similarity

INTERPRO:IPR006047

F

From TAIR

GO:0005975

carbohydrate metabolic process

TAIR:AnalysisReference:501748310

IEA: Inferred from Electronic Annotation

INTERPRO:IPR004193
INTERPRO:IPR006047
INTERPRO:IPR011839
INTERPRO:IPR013781

P

From TAIR

GO:0005975

carbohydrate metabolic process

TAIR:Communication:501714663

ISS: Inferred from Sequence or Structural Similarity

INTERPRO:IPR006047

P

From TAIR

GO:0005983

starch catabolic process

TAIR:Publication:501716563
PMID:15862090[1]

TAS: Traceable Author Statement

P

From TAIR

GO:0005983

starch catabolic process

TAIR:Publication:501728658
PMID:18815382[2]

IMP: Inferred from Mutant Phenotype

P

From TAIR

GO:0005983

starch catabolic process

TAIR:Publication:501735335
PMID:19776162[3]

IMP: Inferred from Mutant Phenotype

P

From TAIR

GO:0009507

chloroplast

TAIR:Publication:501712079
PMID:15028209[4]

IDA: Inferred from Direct Assay

C

From TAIR

GO:0009507

chloroplast

TAIR:Publication:501724486
PMID:18431481[5]

IDA: Inferred from Direct Assay

C

From TAIR

GO:0009570

chloroplast stroma

TAIR:Publication:501735990
PMID:20061580[6]

IDA: Inferred from Direct Assay

C

From TAIR

GO:0010303

limit dextrinase activity

TAIR:Publication:501715219
PMID:15849301[7]

IDA: Inferred from Direct Assay

F

From TAIR

GO:0019252

starch biosynthetic process

TAIR:Publication:501728658
PMID:18815382[2]

IMP: Inferred from Mutant Phenotype

P

From TAIR

GO:0043169

cation binding

TAIR:AnalysisReference:501748310

IEA: Inferred from Electronic Annotation

INTERPRO:IPR006047
INTERPRO:IPR013781

F

From TAIR

GO:0051060

pullulanase activity

TAIR:AnalysisReference:501748310

IEA: Inferred from Electronic Annotation

INTERPRO:IPR011839

F

From TAIR

GO:0051060

pullulanase activity

TAIR:Publication:501728658
PMID:18815382[2]

IDA: Inferred from Direct Assay

F

From TAIR


Notes

References

See Help:References for how to manage references in GONUTS.

  1. Smith AM et al. (2005) Starch degradation. Annu Rev Plant Biol 56: 73-98 PubMed GONUTS page
  2. 2.0 2.1 2.2 Wattebled F et al. (2008) 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. Plant Physiol 148: 1309-23 PubMed GONUTS page
  3. Streb S et al. (2009) The debate on the pathway of starch synthesis: a closer look at low-starch mutants lacking plastidial phosphoglucomutase supports the chloroplast-localized pathway. Plant Physiol 151: 1769-72 PubMed GONUTS page
  4. Kleffmann T et al. (2004) The Arabidopsis thaliana chloroplast proteome reveals pathway abundance and novel protein functions. Curr Biol 14: 354-62 PubMed GONUTS page
  5. Zybailov B et al. (2008) Sorting signals, N-terminal modifications and abundance of the chloroplast proteome. PLoS One 3: e1994 PubMed GONUTS page
  6. Ferro M et al. (2010) AT_CHLORO, a comprehensive chloroplast proteome database with subplastidial localization and curated information on envelope proteins. Mol Cell Proteomics 9: 1063-84 PubMed GONUTS page
  7. Wattebled F et al. (2005) Mutants of Arabidopsis lacking a chloroplastic isoamylase accumulate phytoglycogen and an abnormal form of amylopectin. Plant Physiol 138: 184-95 PubMed GONUTS page


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