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

Q93ZI4 (BGL10_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 78. 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 10

Short name=AtBGLU10
EC=3.2.1.21
Gene names
Name:BGLU10
Ordered Locus Names:At4g27830
ORF Names:T27E11.70
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length508 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.

Sequence similarities

Belongs to the glycosyl hydrolase 1 family.

Sequence caution

The sequence CAB43971.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB81432.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 508486Beta-glucosidase 10
PRO_0000389572

Regions

Region448 – 4492Substrate binding By similarity

Sites

Active site1881Proton donor By similarity
Active site3981Nucleophile By similarity
Binding site421Substrate By similarity
Binding site1421Substrate By similarity
Binding site1871Substrate By similarity
Binding site3311Substrate By similarity
Binding site4411Substrate By similarity

Amino acid modifications

Glycosylation2141N-linked (GlcNAc...) Potential
Glycosylation2191N-linked (GlcNAc...) Potential
Glycosylation3651N-linked (GlcNAc...) Potential
Glycosylation4311N-linked (GlcNAc...) Potential
Glycosylation4631N-linked (GlcNAc...) Potential
Glycosylation4851N-linked (GlcNAc...) Potential
Glycosylation5011N-linked (GlcNAc...) Potential
Disulfide bond207 ↔ 215 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q93ZI4 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 47458C35740A6D20

FASTA50857,078
        10         20         30         40         50         60 
MKLYSLLSVF LVILLATSDS DAFTRNNFPK DFLFGAATSA YQWEGAVAED GRTPSVWDTF 

        70         80         90        100        110        120 
SHTYNRGNLG NGDITSDGYH KYKEDVKLMA EMGLESFRFS ISWSRLIPNG RGLINPKGLL 

       130        140        150        160        170        180 
FYKNLIKELI SHGIEPHVTL YHYDLPQSLE DEYGGWINRK IIEDFTAYAD VCFREFGEDV 

       190        200        210        220        230        240 
KLWTTINEAT IFAIGSYDQG ISPPGHCSPN KFINCTSGNS STEPYLAGHN ILLAHASASK 

       250        260        270        280        290        300 
LYKLKYKSTQ KGSIGLSIFA FGLSPYTNSK DDEIATQRAK AFFYGWMLKP LVFGDYPDEM 

       310        320        330        340        350        360 
KRTVGSRLPV FSEEESEQLK GSSDFIGIIH YTTFYVTNKP SPSIFPSMNE GFFKDMGVYM 

       370        380        390        400        410        420 
ISAANSSFLL WEATPWGLEG ILEYIKQSYN NPPIYILENG MPMGRDSTLQ DTQRIEFIQA 

       430        440        450        460        470        480 
YIGAMLNAIK NGSDTRGYFV WSMIDLYELL SGYTTSFGMY YVNFSDPGRK RTPKLSASWY 

       490        500 
TGFLNGTIDV ATQDTIQLQS NISGSSSL 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [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]"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.
[4]"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.
[5]"The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic diversity."
Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M., Tohge T., Fernie A.R.
Plant Physiol. Biochem. 0:0-0(2013)
Cited for: REVIEW, NOMENCLATURE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL078579 Genomic DNA. Translation: CAB43971.1. Sequence problems.
AL161571 Genomic DNA. Translation: CAB81432.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE85398.1.
AY057518 mRNA. Translation: AAL09758.1.
BT002654 mRNA. Translation: AAO11570.1.
PIRT09022.
RefSeqNP_567787.1. NM_118921.3.
UniGeneAt.23641.

3D structure databases

ProteinModelPortalQ93ZI4.
SMRQ93ZI4. Positions 24-484.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT4G27830.1-P.

Protein family/group databases

CAZyGH1. Glycoside Hydrolase Family 1.

Proteomic databases

PaxDbQ93ZI4.
PRIDEQ93ZI4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G27830.1; AT4G27830.1; AT4G27830.
GeneID828896.
KEGGath:AT4G27830.

Organism-specific databases

TAIRAT4G27830.

Phylogenomic databases

eggNOGCOG2723.
HOGENOMHOG000088630.
InParanoidQ93ZI4.
KOK01188.
OMANKFINCT.
PhylomeDBQ93ZI4.

Enzyme and pathway databases

BioCycARA:AT4G27830-MONOMER.
MetaCyc:MONOMER-18515.

Gene expression databases

GenevestigatorQ93ZI4.

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 nameBGL10_ARATH
AccessionPrimary (citable) accession number: Q93ZI4
Secondary accession number(s): Q9STP3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 24, 2009
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 78 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