Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9M1C9 (BGL30_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Beta-glucosidase 30

Short name=AtBGLU30
EC=3.2.1.21
Alternative name(s):
Protein DARK INDUCIBLE 2
Protein SENESCENCE-RELATED GENE 2
Gene names
Name:BGLU30
Synonyms:DIN2, SRG2
Ordered Locus Names:At3g60140
ORF Names:T2O9.120
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length577 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

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

Induction

By sucrose starvation, dark and senescence. Ref.1 Ref.6

Sequence similarities

Belongs to the glycosyl hydrolase 1 family.

Sequence caution

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

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

Ontologies

Keywords
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionbeta-glucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 577554Beta-glucosidase 30
PRO_0000389592

Regions

Region467 – 4682Substrate binding By similarity

Sites

Active site1941Proton donor By similarity
Active site4101Nucleophile By similarity
Binding site451Substrate By similarity
Binding site1481Substrate By similarity
Binding site1931Substrate By similarity
Binding site3381Substrate By similarity
Binding site4601Substrate By similarity

Amino acid modifications

Glycosylation3281N-linked (GlcNAc...) Potential
Glycosylation3681N-linked (GlcNAc...) Potential
Glycosylation5241N-linked (GlcNAc...) Potential
Glycosylation5441N-linked (GlcNAc...) Potential
Disulfide bond213 ↔ 221 By similarity

Experimental info

Sequence conflict521E → K in AAG23719. Ref.1
Sequence conflict64 – 663SLT → TLS in AAK32907. Ref.4
Sequence conflict891D → G in AAK32907. Ref.4
Sequence conflict891D → G in AAM91436. Ref.4
Sequence conflict1081S → A in AAK32907. Ref.4
Sequence conflict2271S → R in AAK32907. Ref.4
Sequence conflict2481F → I in AAK32907. Ref.4
Sequence conflict3341G → R in AAK32907. Ref.4
Sequence conflict3341G → R in AAM91436. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9M1C9 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: BAD5112154DB1E11

FASTA57766,920
        10         20         30         40         50         60 
MAKGSWFFII LFIISMLENM INSLELDRHS FPDDFIFGTA ASAFQYEGAT SEGGKSPTIW 

        70         80         90        100        110        120 
DHFSLTYPER TKMHNADVAI DFYHRYKDDI KLMKELNMDA FRFSISWSRL IPSGKLKDGV 

       130        140        150        160        170        180 
NKEGVQFYKD LIDELLANDI QPSMTLYHWD HPQSLEDEYG GFLSPKIVED FRDFARICFE 

       190        200        210        220        230        240 
EFGDKVKMWT TINEPYIMTV AGYDQGNKAA GRCSKWVNEK CQAGDSSTEP YIVSHHTLLA 

       250        260        270        280        290        300 
HAAAVEEFRK CEKTSHDGQI GIVLSPRWFE PYHSDSTDDK EAAERALAFE IGWHLDPVIH 

       310        320        330        340        350        360 
GDYPEIVKKY AGNKLPSFTV EQSKMLQNSS DFVGINYYTA RFAAHLPHID PEKPRFKTDH 

       370        380        390        400        410        420 
HVEWKLTNHS GHIIGPGEER GFLFSHPEGL RKVLNYIKER YNNMPVYIKE NGINDNDDGT 

       430        440        450        460        470        480 
KPREEIVKDT FRIEYHKTHF EELHKAIVED GCDVRGYYAW SLMDNFEWEH GYTARFGLYY 

       490        500        510        520        530        540 
VDFVNGLKRY PKDSVKWFKR FLKKSVVGES NKEEVEEMSR AEGNKTFKGF EESAGFFASF 

       550        560        570 
MAMNQSRRDE ENNRCSFDFP HTHFGVLQGI ENPSSFY 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase family 1."
Xu Z., Escamilla-Trevino L.L., Zeng L., Lalgondar M., Bevan D.R., Winkel B.S.J., Mohamed A., Cheng C.-L., Shih M.-C., Poulton J.E., Esen A.
Plant Mol. Biol. 55:343-367(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT47838.
RefSeqNP_191573.1. NM_115877.3.
UniGeneAt.1182.

3D structure databases

ProteinModelPortalQ9M1C9.
SMRQ9M1C9. Positions 25-504.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT3G60140.1-P.

Protein family/group databases

CAZyGH1. Glycoside Hydrolase Family 1.

Proteomic databases

PaxDbQ9M1C9.
PRIDEQ9M1C9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G60140.1; AT3G60140.1; AT3G60140.
GeneID825184.
KEGGath:AT3G60140.

Organism-specific databases

TAIRAT3G60140.

Phylogenomic databases

eggNOGCOG2723.
HOGENOMHOG000088630.
InParanoidQ9M1C9.
KOK01188.
OMAMEPEDER.
PhylomeDBQ9M1C9.
ProtClustDBCLSN2680239.

Enzyme and pathway databases

BioCycARA:AT3G60140-MONOMER.

Gene expression databases

GenevestigatorQ9M1C9.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR10353. PTHR10353. 1 hit.
PfamPF00232. Glyco_hydro_1. 1 hit.
[Graphical view]
PRINTSPR00131. GLHYDRLASE1.
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBGL30_ARATH
AccessionPrimary (citable) accession number: Q9M1C9
Secondary accession number(s): Q39225 expand/collapse secondary AC list , Q39226, Q8L7I3, Q9ASR7, Q9FVM4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 24, 2009
Last sequence update: October 1, 2000
Last modified: February 19, 2014
This is version 77 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names