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Q9LZS3 (GLGB2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 93. 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 2-2, chloroplastic/amyloplastic

Short name=AtSBE II-2
EC=2.4.1.18
Alternative name(s):
Branching enzyme 2
Short name=AtBE2
Starch-branching enzyme 2-2
Gene names
Name:SBE2.2
Synonyms:BE2
Ordered Locus Names:At5g03650
ORF Names:F17C15.70
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length805 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.7

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.6 Ref.9 Ref.11 Ref.12.

Tissue specificity

Expressed in seedlings, roots, stems, leaves, inflorescences, seeds and flowers. Ref.4 Ref.8

Induction

Induced by light when associated with glucose, fructose or sucrose treatment. Induction by glucose is mediated by the transcription factor ABI4. Ref.3 Ref.10

Disruption phenotype

Modified starch composition. This phenotype is enhanced when associated with SBE2.1 and SBE3 disruptions. Ref.7

Sequence similarities

Belongs to the glycosyl hydrolase 13 family. GlgB subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3232Chloroplast By similarity
Chain33 – 8057731,4-alpha-glucan-branching enzyme 2-2, chloroplastic/amyloplastic
PRO_0000415336

Sites

Active site4511Nucleophile By similarity
Active site5061Proton donor By similarity

Experimental info

Sequence conflict6 – 72GV → RS in AAB03100. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9LZS3 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 7CE130BD9C4941D0

FASTA80592,591
        10         20         30         40         50         60 
MVVIHGVSLT PRFTLPSRPL NTGFNAGNST LSFFFKKHPL SRKIFAGKQS AEFDSSSQAI 

        70         80         90        100        110        120 
SASEKVLVPD NLDDDPRGFS QIFDLESQTM EYTEAVRTED QTMNVVKERG VKPRIVPPPG 

       130        140        150        160        170        180 
DGKKIYEIDP MLRTYNNHLD YRYGQYKRLR EEIDKYEGGL EAFSRGYEKL GFSRSDAGIT 

       190        200        210        220        230        240 
YREWAPGAKA ASLIGDFNNW NSNADIMTRN EFGVWEIFLP NNTDGSPAIP HGSRVKIRMD 

       250        260        270        280        290        300 
TPSGIKDSIP AWIKFSVQAP GEIPFNGIYY DPPEEEKYVF KHPQPKRPKS LRIYEAHVGM 

       310        320        330        340        350        360 
SSTEPMVNTY ANFRDDVLPR IKKLGYNAVQ IMAIQEHSYY ASFGYHVTNF FAPSSRCGTP 

       370        380        390        400        410        420 
EELKSLIDRA HELGLVVLMD IVHSHASKNT LDGLNMFDGT DAHYFHSGPR GYHWMWDSRL 

       430        440        450        460        470        480 
FNYGSWEVLR YLLSNARWWL EEYKFDGFRF DGVTSMMYTH HGLSVGFTGN YTEYFGLETD 

       490        500        510        520        530        540 
VDAVNYLMLV NDMIHGLYPE AITVGEDVSG MPTFCIPVQD GGVGFDYRLH MAIADKWIEM 

       550        560        570        580        590        600 
LKKRDEDWQM GDIIYTLTNR RWSEKCISYA ESHDQALVGD KTIAFWLMDK DMYDFMAVDR 

       610        620        630        640        650        660 
PSTPLIDRGI ALHKMIRLIT MGLGGEGYLN FMGNEFGHPE WIDFPRGEQR LSDGSVIPGN 

       670        680        690        700        710        720 
NFSYDKCRRR FDLGDADYLR YRGLQEFDQA MQHLEENYGF MTSEHQFISR KDEADRVIVF 

       730        740        750        760        770        780 
ERGDLVFVFN FHWTSSYFDY RIGCSKPGKY KIVLDSDDPL FGGFNRLDRK AEYFTYDGLY 

       790        800 
DERPCSFMVY APCRTAVVYA LANHD 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Functional annotation of a full-length Arabidopsis cDNA collection."
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K.
Science 296:141-145(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 589-805.
Strain: cv. Columbia.
[6]"The oligomeric stromal proteome of Arabidopsis thaliana chloroplasts."
Peltier J.-B., Cai Y., Sun Q., Zabrouskov V., Giacomelli L., Rudella A., Ytterberg A.J., Rutschow H., van Wijk K.J.
Mol. Cell. Proteomics 5:114-133(2006) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS65046.
T48392.
RefSeqNP_195985.3. NM_120446.3.
UniGeneAt.24317.
At.4765.

3D structure databases

ProteinModelPortalQ9LZS3.
SMRQ9LZS3. Positions 121-799.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT5G03650.1-P.

Protein family/group databases

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

Proteomic databases

PRIDEQ9LZS3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G03650.1; AT5G03650.1; AT5G03650.
GeneID831769.
KEGGath:AT5G03650.

Organism-specific databases

TAIRAT5G03650.

Phylogenomic databases

eggNOGCOG0296.
HOGENOMHOG000175159.
InParanoidQ9LZS3.
KOK00700.
OMANRRWSEK.
PhylomeDBQ9LZS3.

Enzyme and pathway databases

BioCycARA:AT5G03650-MONOMER.
UniPathwayUPA00152.

Gene expression databases

GenevestigatorQ9LZS3.

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...

Other

PROQ9LZS3.

Entry information

Entry nameGLGB2_ARATH
AccessionPrimary (citable) accession number: Q9LZS3
Secondary accession number(s): O81711, Q42531, Q8GYC4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 93 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