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Protein

1,4-alpha-glucan-branching enzyme 2-1, chloroplastic/amyloplastic

Gene

SBE2.1

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

Functioni

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.1 Publication

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei486 – 4861NucleophileBy similarity
Active sitei541 – 5411Proton donorBy similarity

GO - Molecular functioni

  1. 1,4-alpha-glucan branching enzyme activity Source: TAIR
  2. cation binding Source: InterPro
  3. hydrolase activity, hydrolyzing O-glycosyl compounds Source: InterPro

GO - Biological processi

  1. amylopectin biosynthetic process Source: TAIR
  2. cellular response to fructose stimulus Source: UniProtKB
  3. cellular response to glucose stimulus Source: UniProtKB
  4. cellular response to light stimulus Source: UniProtKB
  5. cellular response to sucrose stimulus Source: UniProtKB
  6. glycogen biosynthetic process Source: InterPro
  7. starch biosynthetic process Source: UniProtKB-UniPathway
  8. starch metabolic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciARA:AT2G36390-MONOMER.
UniPathwayiUPA00152.

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
1,4-alpha-glucan-branching enzyme 2-1, chloroplastic/amyloplastic (EC:2.4.1.18)
Short name:
AtSBE II-1
Alternative name(s):
Branching enzyme 3
Short name:
AtBE3
Starch-branching enzyme 2-1
Gene namesi
Name:SBE2.1
Synonyms:BE3
Ordered Locus Names:At2g36390
ORF Names:F1O11.2
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G36390.

Subcellular locationi

  1. Plastidchloroplast stroma 4 Publications
  2. Plastidamyloplast By similarity

GO - Cellular componenti

  1. amyloplast Source: UniProtKB-SubCell
  2. chloroplast Source: TAIR
  3. chloroplast stroma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Amyloplast, Chloroplast, Plastid

Pathology & Biotechi

Disruption phenotypei

Modified starch composition. This phenotype is enhanced when associated with SBE2.2 and SBE3 disruptions.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3737ChloroplastSequence AnalysisAdd
BLAST
Chaini38 – 8588211,4-alpha-glucan-branching enzyme 2-1, chloroplastic/amyloplasticPRO_0000415335Add
BLAST

Proteomic databases

PaxDbiO23647.
PRIDEiO23647.

Expressioni

Tissue specificityi

Mostly expressed in roots, stems, seeds, inflorescences, flowers and leaves, and, to a lower extent, in seedlings.2 Publications

Inductioni

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

Gene expression databases

GenevestigatoriO23647.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi3702.AT2G36390.1-P.

Structurei

3D structure databases

ProteinModelPortaliO23647.
SMRiO23647. Positions 177-838.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi838 – 8436Poly-Asp

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0296.
HOGENOMiHOG000175159.
InParanoidiO23647.
KOiK00700.
OMAiIDFPRTD.
PhylomeDBiO23647.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. 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]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PF02922. CBM_48. 1 hit.
[Graphical view]
PIRSFiPIRSF000463. GlgB. 1 hit.
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.

Sequencei

Sequence statusi: Complete.

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

O23647-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVYTISGVRF PHLPSIKKKN SSLHSFNEDL RRSNAVSFSL RKDSRSSGKV
60 70 80 90 100
FARKPSYDSD SSSLATTASE KLRGHQSDSS SSASDQVQSR DTVSDDTQVL
110 120 130 140 150
GNVDVQKTEE AQETETLDQT SALSTSGSIS YKEDFAKMSH SVDQEVGQRK
160 170 180 190 200
IPPPGDGKRI YDIDPMLNSH RNHLDYRYGQ YRKLREEIDK NEGGLEAFSR
210 220 230 240 250
GYEIFGFTRS ATGITYREWA PGAKAASLIG DFNNWNAKSD VMARNDFGVW
260 270 280 290 300
EIFLPNNADG SPAIPHGSRV KIRMDTPSGI KDSIPAWIKY SVQPPGEIPY
310 320 330 340 350
NGVYYDPPEE DKYAFKHPRP KKPTSLRIYE SHVGMSSTEP KINTYANFRD
360 370 380 390 400
DVLPRIKKLG YNAVQIMAIQ EHAYYASFGY HVTNFFAPSS RFGTPDDLKS
410 420 430 440 450
LIDKAHELGL VVLMDIVHSH ASKNTLDGLD MFDGTDGQYF HSGSRGYHWM
460 470 480 490 500
WDSRLFNYGS WEVLRYLLSN ARWWLEEYKF DGFRFDGVTS MMYTHHGLQV
510 520 530 540 550
EFTGNYNEYF GYSTDVDAVV YLMLVNDLIH GLYPEAIVVG EDVSGMPAFC
560 570 580 590 600
VPVEDGGVGF DYRLHMAVAD KWIELLKKRD EDWQVGDITF TLTNRRWGEK
610 620 630 640 650
CVVYAESHDQ ALVGDKTIAF WLMDKDMYDF MAVDRQATPR VDRGIALHKM
660 670 680 690 700
IRLITMGLGG EGYLNFMGNE FGHPEWIDFP RTDQHLPDGR VIAGNNGSYD
710 720 730 740 750
KCRRRFDLGD AEYLRYHGLQ EFDRAMQNLE ETYGFMTSEH QYISRKDEGD
760 770 780 790 800
RVIVFERGNL LFVFNFHWTN SYSDYRIGCS VPGKYKIVLD SDNSLFGGFN
810 820 830 840 850
RLDDSAEFFT SDGRHDDRPC SFMVYAPCRT AVVYAAVDDD DDDERSSLVP

IGLLPEDV
Length:858
Mass (Da):97,660
Last modified:January 1, 1998 - v1
Checksum:iE1D61C0C21D456F1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 73ISG → RAR in AAB03099 (PubMed:8616246).Curated
Sequence conflicti453 – 4531S → T in AAB03099 (PubMed:8616246).Curated
Sequence conflicti702 – 7021C → S in AAB03099 (PubMed:8616246).Curated
Sequence conflicti745 – 7451R → P in AAB03099 (PubMed:8616246).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiB84780.
S65045.
RefSeqiNP_181180.1. NM_129196.3.
UniGeneiAt.24317.
At.67284.

Genome annotation databases

EnsemblPlantsiAT2G36390.1; AT2G36390.1; AT2G36390.
GeneIDi818212.
KEGGiath:AT2G36390.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiB84780.
S65045.
RefSeqiNP_181180.1. NM_129196.3.
UniGeneiAt.24317.
At.67284.

3D structure databases

ProteinModelPortaliO23647.
SMRiO23647. Positions 177-838.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT2G36390.1-P.

Protein family/group databases

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

Proteomic databases

PaxDbiO23647.
PRIDEiO23647.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G36390.1; AT2G36390.1; AT2G36390.
GeneIDi818212.
KEGGiath:AT2G36390.

Organism-specific databases

TAIRiAT2G36390.

Phylogenomic databases

eggNOGiCOG0296.
HOGENOMiHOG000175159.
InParanoidiO23647.
KOiK00700.
OMAiIDFPRTD.
PhylomeDBiO23647.

Enzyme and pathway databases

UniPathwayiUPA00152.
BioCyciARA:AT2G36390-MONOMER.

Miscellaneous databases

PROiO23647.

Gene expression databases

GenevestigatoriO23647.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. 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]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PF02922. CBM_48. 1 hit.
[Graphical view]
PIRSFiPIRSF000463. GlgB. 1 hit.
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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.
    , 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.

Entry informationi

Entry nameiGLGB1_ARATH
AccessioniPrimary (citable) accession number: O23647
Secondary accession number(s): Q42526
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: January 1, 1998
Last modified: April 29, 2015
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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

External Data

Dasty 3

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 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.