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Protein

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

Gene

SBE2.2

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.

Pathway: starch biosynthesis

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei451 – 4511NucleophileBy similarity
Active sitei506 – 5061Proton donorBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciARA:AT5G03650-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 2-2, chloroplastic/amyloplastic (EC:2.4.1.18)
Short name:
AtSBE II-2
Alternative name(s):
Branching enzyme 2
Short name:
AtBE2
Starch-branching enzyme 2-2
Gene namesi
Name:SBE2.2
Synonyms:BE2
Ordered Locus Names:At5g03650
ORF Names:F17C15.70
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G03650.

Subcellular locationi

GO - Cellular componenti

  • amyloplast Source: UniProtKB-SubCell
  • chloroplast Source: TAIR
  • 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 SBE2.1 and SBE3 disruptions.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3232ChloroplastBy similarityAdd
BLAST
Chaini33 – 8057731,4-alpha-glucan-branching enzyme 2-2, chloroplastic/amyloplasticPRO_0000415336Add
BLAST

Proteomic databases

PRIDEiQ9LZS3.

Expressioni

Tissue specificityi

Expressed in seedlings, roots, stems, leaves, inflorescences, seeds and flowers.2 Publications

Inductioni

Induced by light when associated with glucose, fructose or sucrose treatment. Induction by glucose is mediated by the transcription factor ABI4.2 Publications

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi17045. 1 interaction.
STRINGi3702.AT5G03650.1.

Structurei

3D structure databases

ProteinModelPortaliQ9LZS3.
SMRiQ9LZS3. Positions 121-799.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0296.
HOGENOMiHOG000175159.
InParanoidiQ9LZS3.
KOiK00700.
OMAiAMVYLML.
PhylomeDBiQ9LZS3.

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.

Q9LZS3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVVIHGVSLT PRFTLPSRPL NTGFNAGNST LSFFFKKHPL SRKIFAGKQS
60 70 80 90 100
AEFDSSSQAI SASEKVLVPD NLDDDPRGFS QIFDLESQTM EYTEAVRTED
110 120 130 140 150
QTMNVVKERG VKPRIVPPPG DGKKIYEIDP MLRTYNNHLD YRYGQYKRLR
160 170 180 190 200
EEIDKYEGGL EAFSRGYEKL GFSRSDAGIT YREWAPGAKA ASLIGDFNNW
210 220 230 240 250
NSNADIMTRN EFGVWEIFLP NNTDGSPAIP HGSRVKIRMD TPSGIKDSIP
260 270 280 290 300
AWIKFSVQAP GEIPFNGIYY DPPEEEKYVF KHPQPKRPKS LRIYEAHVGM
310 320 330 340 350
SSTEPMVNTY ANFRDDVLPR IKKLGYNAVQ IMAIQEHSYY ASFGYHVTNF
360 370 380 390 400
FAPSSRCGTP EELKSLIDRA HELGLVVLMD IVHSHASKNT LDGLNMFDGT
410 420 430 440 450
DAHYFHSGPR GYHWMWDSRL FNYGSWEVLR YLLSNARWWL EEYKFDGFRF
460 470 480 490 500
DGVTSMMYTH HGLSVGFTGN YTEYFGLETD VDAVNYLMLV NDMIHGLYPE
510 520 530 540 550
AITVGEDVSG MPTFCIPVQD GGVGFDYRLH MAIADKWIEM LKKRDEDWQM
560 570 580 590 600
GDIIYTLTNR RWSEKCISYA ESHDQALVGD KTIAFWLMDK DMYDFMAVDR
610 620 630 640 650
PSTPLIDRGI ALHKMIRLIT MGLGGEGYLN FMGNEFGHPE WIDFPRGEQR
660 670 680 690 700
LSDGSVIPGN NFSYDKCRRR FDLGDADYLR YRGLQEFDQA MQHLEENYGF
710 720 730 740 750
MTSEHQFISR KDEADRVIVF ERGDLVFVFN FHWTSSYFDY RIGCSKPGKY
760 770 780 790 800
KIVLDSDDPL FGGFNRLDRK AEYFTYDGLY DERPCSFMVY APCRTAVVYA

LANHD
Length:805
Mass (Da):92,591
Last modified:October 1, 2000 - v1
Checksum:i7CE130BD9C4941D0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 72GV → RS in AAB03100 (PubMed:8616246).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL162506 Genomic DNA. Translation: CAB82930.1.
CP002688 Genomic DNA. Translation: AED90637.1.
AJ005130 Genomic DNA. Translation: CAA06392.1.
U22428 mRNA. Translation: AAB03100.1.
AK117729 mRNA. Translation: BAC42378.1.
PIRiS65046.
T48392.
RefSeqiNP_195985.3. NM_120446.3.
UniGeneiAt.24317.
At.4765.

Genome annotation databases

EnsemblPlantsiAT5G03650.1; AT5G03650.1; AT5G03650.
GeneIDi831769.
KEGGiath:AT5G03650.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL162506 Genomic DNA. Translation: CAB82930.1.
CP002688 Genomic DNA. Translation: AED90637.1.
AJ005130 Genomic DNA. Translation: CAA06392.1.
U22428 mRNA. Translation: AAB03100.1.
AK117729 mRNA. Translation: BAC42378.1.
PIRiS65046.
T48392.
RefSeqiNP_195985.3. NM_120446.3.
UniGeneiAt.24317.
At.4765.

3D structure databases

ProteinModelPortaliQ9LZS3.
SMRiQ9LZS3. Positions 121-799.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi17045. 1 interaction.
STRINGi3702.AT5G03650.1.

Protein family/group databases

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

Proteomic databases

PRIDEiQ9LZS3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G03650.1; AT5G03650.1; AT5G03650.
GeneIDi831769.
KEGGiath:AT5G03650.

Organism-specific databases

TAIRiAT5G03650.

Phylogenomic databases

eggNOGiCOG0296.
HOGENOMiHOG000175159.
InParanoidiQ9LZS3.
KOiK00700.
OMAiAMVYLML.
PhylomeDBiQ9LZS3.

Enzyme and pathway databases

UniPathwayiUPA00152.
BioCyciARA:AT5G03650-MONOMER.

Miscellaneous databases

PROiQ9LZS3.

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. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [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. "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] OF 1-81, INDUCTION BY LIGHT.
    Strain: cv. Columbia.
  4. "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 6-805, TISSUE SPECIFICITY.
    Strain: cv. Columbia.
    Tissue: Seedling hypocotyl.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 589-805.
    Strain: cv. Columbia.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. "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. Wassilewskija.
  8. "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.
  9. "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.
  10. "The Arabidopsis ABA-INSENSITIVE (ABI) 4 factor acts as a central transcription activator of the expression of its own gene, and for the induction of ABI5 and SBE2.2 genes during sugar signaling."
    Bossi F., Cordoba E., Dupre P., Mendoza M.S., Roman C.S., Leon P.
    Plant J. 59:359-374(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY GLUCOSE.
    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 [LARGE SCALE ANALYSIS].
    Strain: cv. Columbia.

Entry informationi

Entry nameiGLGB2_ARATH
AccessioniPrimary (citable) accession number: Q9LZS3
Secondary accession number(s): O81711, Q42531, Q8GYC4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: October 1, 2000
Last modified: June 24, 2015
This is version 97 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.