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Q9M1C9

- BGL30_ARATH

UniProt

Q9M1C9 - BGL30_ARATH

Protein

Beta-glucosidase 30

Gene

BGLU30

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei45 – 451SubstrateBy similarity
    Binding sitei148 – 1481SubstrateBy similarity
    Binding sitei193 – 1931SubstrateBy similarity
    Active sitei194 – 1941Proton donorBy similarity
    Binding sitei338 – 3381SubstrateBy similarity
    Active sitei410 – 4101NucleophileBy similarity
    Binding sitei460 – 4601SubstrateBy similarity

    GO - Molecular functioni

    1. beta-glucosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BioCyciARA:AT3G60140-MONOMER.

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-glucosidase 30 (EC:3.2.1.21)
    Short name:
    AtBGLU30
    Alternative name(s):
    Protein DARK INDUCIBLE 2
    Protein SENESCENCE-RELATED GENE 2
    Gene namesi
    Name:BGLU30
    Synonyms:DIN2, SRG2
    Ordered Locus Names:At3g60140
    ORF Names:T2O9.120
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G60140.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 577554Beta-glucosidase 30PRO_0000389592Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi213 ↔ 221By similarity
    Glycosylationi328 – 3281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi368 – 3681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi524 – 5241N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi544 – 5441N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9M1C9.
    PRIDEiQ9M1C9.

    Expressioni

    Inductioni

    By sucrose starvation, dark and senescence.2 Publications

    Gene expression databases

    GenevestigatoriQ9M1C9.

    Interactioni

    Protein-protein interaction databases

    STRINGi3702.AT3G60140.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9M1C9.
    SMRiQ9M1C9. Positions 25-504.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni467 – 4682Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 1 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2723.
    HOGENOMiHOG000088630.
    InParanoidiQ9M1C9.
    KOiK01188.
    OMAiYRIRYLN.
    PhylomeDBiQ9M1C9.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001360. Glyco_hydro_1.
    IPR018120. Glyco_hydro_1_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10353. PTHR10353. 1 hit.
    PfamiPF00232. Glyco_hydro_1. 1 hit.
    [Graphical view]
    PRINTSiPR00131. GLHYDRLASE1.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9M1C9-1 [UniParc]FASTAAdd to Basket

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    MAKGSWFFII LFIISMLENM INSLELDRHS FPDDFIFGTA ASAFQYEGAT    50
    SEGGKSPTIW DHFSLTYPER TKMHNADVAI DFYHRYKDDI KLMKELNMDA 100
    FRFSISWSRL IPSGKLKDGV NKEGVQFYKD LIDELLANDI QPSMTLYHWD 150
    HPQSLEDEYG GFLSPKIVED FRDFARICFE EFGDKVKMWT TINEPYIMTV 200
    AGYDQGNKAA GRCSKWVNEK CQAGDSSTEP YIVSHHTLLA HAAAVEEFRK 250
    CEKTSHDGQI GIVLSPRWFE PYHSDSTDDK EAAERALAFE IGWHLDPVIH 300
    GDYPEIVKKY AGNKLPSFTV EQSKMLQNSS DFVGINYYTA RFAAHLPHID 350
    PEKPRFKTDH HVEWKLTNHS GHIIGPGEER GFLFSHPEGL RKVLNYIKER 400
    YNNMPVYIKE NGINDNDDGT KPREEIVKDT FRIEYHKTHF EELHKAIVED 450
    GCDVRGYYAW SLMDNFEWEH GYTARFGLYY VDFVNGLKRY PKDSVKWFKR 500
    FLKKSVVGES NKEEVEEMSR AEGNKTFKGF EESAGFFASF MAMNQSRRDE 550
    ENNRCSFDFP HTHFGVLQGI ENPSSFY 577
    Length:577
    Mass (Da):66,920
    Last modified:October 1, 2000 - v1
    Checksum:iBAD5112154DB1E11
    GO

    Sequence cautioni

    The sequence AAK32907.1 differs from that shown. Reason: Intron retention.
    The sequence AAM91436.1 differs from that shown. Reason: Intron retention.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti52 – 521E → K in AAG23719. (PubMed:11080291)Curated
    Sequence conflicti64 – 663SLT → TLS in AAK32907. (PubMed:14593172)Curated
    Sequence conflicti89 – 891D → G in AAK32907. (PubMed:14593172)Curated
    Sequence conflicti89 – 891D → G in AAM91436. (PubMed:14593172)Curated
    Sequence conflicti108 – 1081S → A in AAK32907. (PubMed:14593172)Curated
    Sequence conflicti227 – 2271S → R in AAK32907. (PubMed:14593172)Curated
    Sequence conflicti248 – 2481F → I in AAK32907. (PubMed:14593172)Curated
    Sequence conflicti334 – 3341G → R in AAK32907. (PubMed:14593172)Curated
    Sequence conflicti334 – 3341G → R in AAM91436. (PubMed:14593172)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF159376 mRNA. Translation: AAG23719.1.
    AL138658 Genomic DNA. Translation: CAB75929.1.
    CP002686 Genomic DNA. Translation: AEE80017.1.
    AF367320 mRNA. Translation: AAK32907.1. Sequence problems.
    AY133606 mRNA. Translation: AAM91436.1. Sequence problems.
    X82623 mRNA. Translation: CAA57943.1.
    X82624 mRNA. Translation: CAA57944.1.
    PIRiT47838.
    RefSeqiNP_191573.1. NM_115877.3.
    UniGeneiAt.1182.

    Genome annotation databases

    EnsemblPlantsiAT3G60140.1; AT3G60140.1; AT3G60140.
    GeneIDi825184.
    KEGGiath:AT3G60140.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF159376 mRNA. Translation: AAG23719.1 .
    AL138658 Genomic DNA. Translation: CAB75929.1 .
    CP002686 Genomic DNA. Translation: AEE80017.1 .
    AF367320 mRNA. Translation: AAK32907.1 . Sequence problems.
    AY133606 mRNA. Translation: AAM91436.1 . Sequence problems.
    X82623 mRNA. Translation: CAA57943.1 .
    X82624 mRNA. Translation: CAA57944.1 .
    PIRi T47838.
    RefSeqi NP_191573.1. NM_115877.3.
    UniGenei At.1182.

    3D structure databases

    ProteinModelPortali Q9M1C9.
    SMRi Q9M1C9. Positions 25-504.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT3G60140.1-P.

    Protein family/group databases

    CAZyi GH1. Glycoside Hydrolase Family 1.

    Proteomic databases

    PaxDbi Q9M1C9.
    PRIDEi Q9M1C9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G60140.1 ; AT3G60140.1 ; AT3G60140 .
    GeneIDi 825184.
    KEGGi ath:AT3G60140.

    Organism-specific databases

    TAIRi AT3G60140.

    Phylogenomic databases

    eggNOGi COG2723.
    HOGENOMi HOG000088630.
    InParanoidi Q9M1C9.
    KOi K01188.
    OMAi YRIRYLN.
    PhylomeDBi Q9M1C9.

    Enzyme and pathway databases

    BioCyci ARA:AT3G60140-MONOMER.

    Gene expression databases

    Genevestigatori Q9M1C9.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001360. Glyco_hydro_1.
    IPR018120. Glyco_hydro_1_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    PANTHERi PTHR10353. PTHR10353. 1 hit.
    Pfami PF00232. Glyco_hydro_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00131. GLHYDRLASE1.
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Multiple signaling pathways in gene expression during sugar starvation. Pharmacological analysis of din gene expression in suspension-cultured cells of Arabidopsis."
      Fujiki Y., Ito M., Nishida I., Watanabe A.
      Plant Physiol. 124:1139-1148(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
    2. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
      Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
      , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
      Nature 408:820-822(2000) [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.
      , 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. "Novel molecular markers for late phases of the growth cycle of Arabidopsis thaliana cell-suspension cultures are expressed during organ senescence."
      Callard D., Axelos M., Mazzolini L.
      Plant Physiol. 112:705-715(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 27-88 AND 456-504.
    6. "Dark-inducible genes from Arabidopsis thaliana are associated with leaf senescence and repressed by sugars."
      Fujiki Y., Yoshikawa Y., Sato T., Inada N., Ito M., Nishida I., Watanabe A.
      Physiol. Plantarum 111:345-352(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    7. Cited for: GENE FAMILY, NOMENCLATURE.

    Entry informationi

    Entry nameiBGL30_ARATH
    AccessioniPrimary (citable) accession number: Q9M1C9
    Secondary accession number(s): Q39225
    , Q39226, Q8L7I3, Q9ASR7, Q9FVM4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 24, 2009
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 79 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3