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Q9LZS3

- GLGB2_ARATH

UniProt

Q9LZS3 - GLGB2_ARATH

Protein

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

Gene

SBE2.2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    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 sitei451 – 4511NucleophileBy similarity
    Active sitei506 – 5061Proton 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

    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: Chromosome 5

    Organism-specific databases

    TAIRiAT5G03650.

    Subcellular locationi

    Plastidchloroplast stroma 4 Publications. Plastidamyloplast By similarity

    GO - Cellular componenti

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

    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

    Gene expression databases

    GenevestigatoriQ9LZS3.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    STRINGi3702.AT5G03650.1-P.

    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.
    OMAiNRRWSEK.
    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

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    MVVIHGVSLT PRFTLPSRPL NTGFNAGNST LSFFFKKHPL SRKIFAGKQS    50
    AEFDSSSQAI SASEKVLVPD NLDDDPRGFS QIFDLESQTM EYTEAVRTED 100
    QTMNVVKERG VKPRIVPPPG DGKKIYEIDP MLRTYNNHLD YRYGQYKRLR 150
    EEIDKYEGGL EAFSRGYEKL GFSRSDAGIT YREWAPGAKA ASLIGDFNNW 200
    NSNADIMTRN EFGVWEIFLP NNTDGSPAIP HGSRVKIRMD TPSGIKDSIP 250
    AWIKFSVQAP GEIPFNGIYY DPPEEEKYVF KHPQPKRPKS LRIYEAHVGM 300
    SSTEPMVNTY ANFRDDVLPR IKKLGYNAVQ IMAIQEHSYY ASFGYHVTNF 350
    FAPSSRCGTP EELKSLIDRA HELGLVVLMD IVHSHASKNT LDGLNMFDGT 400
    DAHYFHSGPR GYHWMWDSRL FNYGSWEVLR YLLSNARWWL EEYKFDGFRF 450
    DGVTSMMYTH HGLSVGFTGN YTEYFGLETD VDAVNYLMLV NDMIHGLYPE 500
    AITVGEDVSG MPTFCIPVQD GGVGFDYRLH MAIADKWIEM LKKRDEDWQM 550
    GDIIYTLTNR RWSEKCISYA ESHDQALVGD KTIAFWLMDK DMYDFMAVDR 600
    PSTPLIDRGI ALHKMIRLIT MGLGGEGYLN FMGNEFGHPE WIDFPRGEQR 650
    LSDGSVIPGN NFSYDKCRRR FDLGDADYLR YRGLQEFDQA MQHLEENYGF 700
    MTSEHQFISR KDEADRVIVF ERGDLVFVFN FHWTSSYFDY RIGCSKPGKY 750
    KIVLDSDDPL FGGFNRLDRK AEYFTYDGLY DERPCSFMVY APCRTAVVYA 800
    LANHD 805
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi S65046.
    T48392.
    RefSeqi NP_195985.3. NM_120446.3.
    UniGenei At.24317.
    At.4765.

    3D structure databases

    ProteinModelPortali Q9LZS3.
    SMRi Q9LZS3. Positions 121-799.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT5G03650.1-P.

    Protein family/group databases

    CAZyi CBM48. Carbohydrate-Binding Module Family 48.
    GH13. Glycoside Hydrolase Family 13.

    Proteomic databases

    PRIDEi Q9LZS3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT5G03650.1 ; AT5G03650.1 ; AT5G03650 .
    GeneIDi 831769.
    KEGGi ath:AT5G03650.

    Organism-specific databases

    TAIRi AT5G03650.

    Phylogenomic databases

    eggNOGi COG0296.
    HOGENOMi HOG000175159.
    InParanoidi Q9LZS3.
    KOi K00700.
    OMAi NRRWSEK.
    PhylomeDBi Q9LZS3.

    Enzyme and pathway databases

    UniPathwayi UPA00152 .
    BioCyci ARA:AT5G03650-MONOMER.

    Miscellaneous databases

    PROi Q9LZS3.

    Gene expression databases

    Genevestigatori Q9LZS3.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    InterProi IPR006048. 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 ]
    PANTHERi PTHR10357. PTHR10357. 1 hit.
    Pfami PF00128. Alpha-amylase. 1 hit.
    PF02806. Alpha-amylase_C. 1 hit.
    PF02922. CBM_48. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000463. GlgB. 1 hit.
    SUPFAMi SSF51445. SSF51445. 1 hit.
    SSF81296. SSF81296. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 94 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