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O23647 (GLGB1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
1,4-alpha-glucan-branching enzyme 2-1, chloroplastic/amyloplastic

Short name=AtSBE II-1
EC=2.4.1.18
Alternative name(s):
Branching enzyme 3
Short name=AtBE3
Starch-branching enzyme 2-1
Gene names
Name:SBE2.1
Synonyms:BE3
Ordered Locus Names:At2g36390
ORF Names:F1O11.2
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length858 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the formation of the alpha-1,6-glucosidic linkages in starch by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position. Ref.8

Catalytic activity

Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain.

Pathway

Glycan biosynthesis; starch biosynthesis.

Subunit structure

Monomer By similarity.

Subcellular location

Plastidchloroplast stroma. Plastidamyloplast By similarity Ref.7 Ref.10 Ref.11 Ref.12.

Tissue specificity

Mostly expressed in roots, stems, seeds, inflorescences, flowers and leaves, and, to a lower extent, in seedlings. Ref.6 Ref.9

Induction

Induced by light, preferentially when associated with glucose, fructose or sucrose treatment, but repressed by darkness. Ref.1

Disruption phenotype

Modified starch composition. This phenotype is enhanced when associated with SBE2.2 and SBE3 disruptions. Ref.8

Sequence similarities

Belongs to the glycosyl hydrolase 13 family. GlgB subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3737Chloroplast Potential
Chain38 – 8588211,4-alpha-glucan-branching enzyme 2-1, chloroplastic/amyloplastic
PRO_0000415335

Regions

Compositional bias838 – 8436Poly-Asp

Sites

Active site4861Nucleophile By similarity
Active site5411Proton donor By similarity

Experimental info

Sequence conflict5 – 73ISG → RAR in AAB03099. Ref.6
Sequence conflict4531S → T in AAB03099. Ref.6
Sequence conflict7021C → S in AAB03099. Ref.6
Sequence conflict7451R → P in AAB03099. Ref.6

Sequences

Sequence LengthMass (Da)Tools
O23647 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: E1D61C0C21D456F1

FASTA85897,660
        10         20         30         40         50         60 
MVYTISGVRF PHLPSIKKKN SSLHSFNEDL RRSNAVSFSL RKDSRSSGKV FARKPSYDSD 

        70         80         90        100        110        120 
SSSLATTASE KLRGHQSDSS SSASDQVQSR DTVSDDTQVL GNVDVQKTEE AQETETLDQT 

       130        140        150        160        170        180 
SALSTSGSIS YKEDFAKMSH SVDQEVGQRK IPPPGDGKRI YDIDPMLNSH RNHLDYRYGQ 

       190        200        210        220        230        240 
YRKLREEIDK NEGGLEAFSR GYEIFGFTRS ATGITYREWA PGAKAASLIG DFNNWNAKSD 

       250        260        270        280        290        300 
VMARNDFGVW EIFLPNNADG SPAIPHGSRV KIRMDTPSGI KDSIPAWIKY SVQPPGEIPY 

       310        320        330        340        350        360 
NGVYYDPPEE DKYAFKHPRP KKPTSLRIYE SHVGMSSTEP KINTYANFRD DVLPRIKKLG 

       370        380        390        400        410        420 
YNAVQIMAIQ EHAYYASFGY HVTNFFAPSS RFGTPDDLKS LIDKAHELGL VVLMDIVHSH 

       430        440        450        460        470        480 
ASKNTLDGLD MFDGTDGQYF HSGSRGYHWM WDSRLFNYGS WEVLRYLLSN ARWWLEEYKF 

       490        500        510        520        530        540 
DGFRFDGVTS MMYTHHGLQV EFTGNYNEYF GYSTDVDAVV YLMLVNDLIH GLYPEAIVVG 

       550        560        570        580        590        600 
EDVSGMPAFC VPVEDGGVGF DYRLHMAVAD KWIELLKKRD EDWQVGDITF TLTNRRWGEK 

       610        620        630        640        650        660 
CVVYAESHDQ ALVGDKTIAF WLMDKDMYDF MAVDRQATPR VDRGIALHKM IRLITMGLGG 

       670        680        690        700        710        720 
EGYLNFMGNE FGHPEWIDFP RTDQHLPDGR VIAGNNGSYD KCRRRFDLGD AEYLRYHGLQ 

       730        740        750        760        770        780 
EFDRAMQNLE ETYGFMTSEH QYISRKDEGD RVIVFERGNL LFVFNFHWTN SYSDYRIGCS 

       790        800        810        820        830        840 
VPGKYKIVLD SDNSLFGGFN RLDDSAEFFT SDGRHDDRPC SFMVYAPCRT AVVYAAVDDD 

       850 
DDDERSSLVP IGLLPEDV 

« Hide

References

« Hide 'large scale' references
[1]"Differential accumulation of Arabidopsis thaliana Sbe 2.1 and Sbe 2.2 transcripts in response to light."
Khoshnoodi J., Larsson C.-T., Larsson H., Rask L.
Plant Sci. 135:183-193(1998)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION BY LIGHT.
Strain: cv. Columbia.
[2]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"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. expand/collapse author list , 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.
[5]"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. expand/collapse author list , 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.
[6]"Two closely related cDNAs encoding starch branching enzyme from Arabidopsis thaliana."
Fisher D.K., Gao M., Kim K.-N., Boyer C.D., Guiltinan M.J.
Plant Mol. Biol. 30:97-108(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-858, TISSUE SPECIFICITY.
Strain: cv. Columbia.
Tissue: Seedling hypocotyl.
[7]"The Arabidopsis thaliana chloroplast proteome reveals pathway abundance and novel protein functions."
Kleffmann T., Russenberger D., von Zychlinski A., Christopher W., Sjoelander K., Gruissem W., Baginsky S.
Curr. Biol. 14:354-362(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[8]"Mutants of Arabidopsis lacking starch branching enzyme II substitute plastidial starch synthesis by cytoplasmic maltose accumulation."
Dumez S., Wattebled F., Dauvillee D., Delvalle D., Planchot V., Ball S.G., D'Hulst C.
Plant Cell 18:2694-2709(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
Strain: cv. Columbia and cv. Wassilewskija.
[9]"Three orthologs in rice, Arabidopsis, and Populus encoding starch branching enzymes (SBEs) are different from other SBE gene families in plants."
Han Y., Sun F.-J., Rosales-Mendoza S., Korban S.S.
Gene 401:123-130(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE.
Strain: cv. Columbia.
[10]"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.
Strain: cv. Columbia.
[11]"AT_CHLORO, a comprehensive chloroplast proteome database with subplastidial localization and curated information on envelope proteins."
Ferro M., Brugiere S., Salvi D., Seigneurin-Berny D., Court M., Moyet L., Ramus C., Miras S., Mellal M., Le Gall S., Kieffer-Jaquinod S., Bruley C., Garin J., Joyard J., Masselon C., Rolland N.
Mol. Cell. Proteomics 9:1063-1084(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Strain: cv. Wassilewskija.
[12]"Megadalton complexes in the chloroplast stroma of Arabidopsis thaliana characterized by size exclusion chromatography, mass spectrometry, and hierarchical clustering."
Olinares P.D., Ponnala L., van Wijk K.J.
Mol. Cell. Proteomics 9:1594-1615(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ000497 Genomic DNA. Translation: CAA04134.1.
AC006919 Genomic DNA. Translation: AAD24644.1.
CP002685 Genomic DNA. Translation: AEC09247.1.
AY136411 mRNA. Translation: AAM97077.1.
AK226896 mRNA. Translation: BAE98973.1.
U18817 mRNA. Translation: AAB03099.1.
PIRB84780.
S65045.
RefSeqNP_181180.1. NM_129196.3.
UniGeneAt.24317.
At.67284.

3D structure databases

ProteinModelPortalO23647.
SMRO23647. Positions 177-838.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT2G36390.1-P.

Protein family/group databases

CAZyCBM48. Carbohydrate-Binding Module Family 48.
GH13. Glycoside Hydrolase Family 13.

Proteomic databases

PaxDbO23647.
PRIDEO23647.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G36390.1; AT2G36390.1; AT2G36390.
GeneID818212.
KEGGath:AT2G36390.

Organism-specific databases

TAIRAT2G36390.

Phylogenomic databases

eggNOGCOG0296.
HOGENOMHOG000175159.
InParanoidO23647.
KOK00700.
OMANEVIHFL.
PhylomeDBO23647.

Enzyme and pathway databases

BioCycARA:AT2G36390-MONOMER.
UniPathwayUPA00152.

Gene expression databases

GenevestigatorO23647.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProIPR006048. A-amylase_b_C.
IPR006407. GlgB.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004193. Glyco_hydro_13_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PF02922. CBM_48. 1 hit.
[Graphical view]
PIRSFPIRSF000463. GlgB. 1 hit.
SUPFAMSSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGLGB1_ARATH
AccessionPrimary (citable) accession number: O23647
Secondary accession number(s): Q42526
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: January 1, 1998
Last modified: May 14, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names