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Q9M1C9

- BGL30_ARATH

UniProt

Q9M1C9 - BGL30_ARATH

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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

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
Complete GO annotation...

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

« Hide

        10         20         30         40         50
MAKGSWFFII LFIISMLENM INSLELDRHS FPDDFIFGTA ASAFQYEGAT
60 70 80 90 100
SEGGKSPTIW DHFSLTYPER TKMHNADVAI DFYHRYKDDI KLMKELNMDA
110 120 130 140 150
FRFSISWSRL IPSGKLKDGV NKEGVQFYKD LIDELLANDI QPSMTLYHWD
160 170 180 190 200
HPQSLEDEYG GFLSPKIVED FRDFARICFE EFGDKVKMWT TINEPYIMTV
210 220 230 240 250
AGYDQGNKAA GRCSKWVNEK CQAGDSSTEP YIVSHHTLLA HAAAVEEFRK
260 270 280 290 300
CEKTSHDGQI GIVLSPRWFE PYHSDSTDDK EAAERALAFE IGWHLDPVIH
310 320 330 340 350
GDYPEIVKKY AGNKLPSFTV EQSKMLQNSS DFVGINYYTA RFAAHLPHID
360 370 380 390 400
PEKPRFKTDH HVEWKLTNHS GHIIGPGEER GFLFSHPEGL RKVLNYIKER
410 420 430 440 450
YNNMPVYIKE NGINDNDDGT KPREEIVKDT FRIEYHKTHF EELHKAIVED
460 470 480 490 500
GCDVRGYYAW SLMDNFEWEH GYTARFGLYY VDFVNGLKRY PKDSVKWFKR
510 520 530 540 550
FLKKSVVGES NKEEVEEMSR AEGNKTFKGF EESAGFFASF MAMNQSRRDE
560 570
ENNRCSFDFP HTHFGVLQGI ENPSSFY
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.Curated
The sequence AAM91436.1 differs from that shown. Reason: Intron retention.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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

« Hide 'large scale' publications
  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