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Q9STP4

- BGL09_ARATH

UniProt

Q9STP4 - BGL09_ARATH

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Protein

Beta-glucosidase 9

Gene

BGLU9

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 sitei42 – 421SubstrateBy similarity
Binding sitei139 – 1391SubstrateBy similarity
Binding sitei184 – 1841SubstrateBy similarity
Active sitei185 – 1851Proton donorBy similarity
Binding sitei328 – 3281SubstrateBy similarity
Active sitei396 – 3961NucleophileBy similarity
Binding sitei439 – 4391SubstrateBy 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:AT4G27820-MONOMER.

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-glucosidase 9 (EC:3.2.1.21)
Short name:
AtBGLU9
Gene namesi
Name:BGLU9
Ordered Locus Names:At4g27820
ORF Names:T27E11.60
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G27820.

Subcellular locationi

GO - Cellular componenti

  1. peroxisome Source: TAIR
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 506484Beta-glucosidase 9PRO_0000389571Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi204 ↔ 212By similarity
Glycosylationi211 – 2111N-linked (GlcNAc...)Sequence Analysis
Glycosylationi216 – 2161N-linked (GlcNAc...)Sequence Analysis
Glycosylationi363 – 3631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi429 – 4291N-linked (GlcNAc...)Sequence Analysis
Glycosylationi461 – 4611N-linked (GlcNAc...)Sequence Analysis
Glycosylationi483 – 4831N-linked (GlcNAc...)Sequence Analysis
Glycosylationi499 – 4991N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9STP4.
PRIDEiQ9STP4.

Expressioni

Gene expression databases

GenevestigatoriQ9STP4.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G27820.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9STP4.
SMRiQ9STP4. Positions 24-482.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni446 – 4472Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyl hydrolase 1 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2723.
HOGENOMiHOG000088630.
InParanoidiQ9STP4.
OMAiNIFAMEG.
PhylomeDBiQ9STP4.

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.

Q9STP4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKHFSLLFIF LVILLATSYS DAFTRNSFPK DFLFGAATSA YQWEGAVAED
60 70 80 90 100
GRTPSVWDTF SNSYDTGNGD VTSDGYHKYK EDVKLMATMG LESFRFSISW
110 120 130 140 150
SRLIPNGRGL INPKGLLFYN NLIKDLKSHG IEPHVTLYHY DLPQSLEDEY
160 170 180 190 200
GGWINRKIIE DFTAYADVCF REFGEDVKLW TTINEATIFA IGSYDQGTAP
210 220 230 240 250
PGHCSPNKFV NCSTGNSSTE PYIAGHNILL AHASASKLYK LKYKSKQKGS
260 270 280 290 300
IGLSIFAFGL SPYTNSKDDE IATQRAKTFL YGWMLKPLVF GDYPDEMKKT
310 320 330 340 350
VGSRLPVFSE EESEQVKGSS DFIGIIHYTT FYVTNHQPSA SLFPSMGEGF
360 370 380 390 400
FKDMGVYIIP TGNSSFLVWE ATPWGLEGIL EYIKQSYNNP PVYILENGMP
410 420 430 440 450
MVRDSTLQDT QRIEYIQAYI DAVLNAMKNG SDTRGYFVWS MVDVYEILSG
460 470 480 490 500
YTTSFGMYHV NFSDPGRKRT PKLSASWYTG FLNGTIDVAS QDTIQLWSNF

SVSSSL
Length:506
Mass (Da):56,892
Last modified:November 24, 2009 - v2
Checksum:iA2841C0D7912EB7C
GO

Sequence cautioni

The sequence CAB43970.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB81431.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL078579 Genomic DNA. Translation: CAB43970.1. Sequence problems.
AL161571 Genomic DNA. Translation: CAB81431.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE85397.1.
AK229513 mRNA. Translation: BAF01368.1.
PIRiT09021.
RefSeqiNP_194511.3. NM_118920.4.
UniGeneiAt.32068.

Genome annotation databases

EnsemblPlantsiAT4G27820.1; AT4G27820.1; AT4G27820.
GeneIDi828895.
KEGGiath:AT4G27820.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL078579 Genomic DNA. Translation: CAB43970.1 . Sequence problems.
AL161571 Genomic DNA. Translation: CAB81431.1 . Sequence problems.
CP002687 Genomic DNA. Translation: AEE85397.1 .
AK229513 mRNA. Translation: BAF01368.1 .
PIRi T09021.
RefSeqi NP_194511.3. NM_118920.4.
UniGenei At.32068.

3D structure databases

ProteinModelPortali Q9STP4.
SMRi Q9STP4. Positions 24-482.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 3702.AT4G27820.1-P.

Protein family/group databases

CAZyi GH1. Glycoside Hydrolase Family 1.

Proteomic databases

PaxDbi Q9STP4.
PRIDEi Q9STP4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G27820.1 ; AT4G27820.1 ; AT4G27820 .
GeneIDi 828895.
KEGGi ath:AT4G27820.

Organism-specific databases

TAIRi AT4G27820.

Phylogenomic databases

eggNOGi COG2723.
HOGENOMi HOG000088630.
InParanoidi Q9STP4.
OMAi NIFAMEG.
PhylomeDBi Q9STP4.

Enzyme and pathway databases

BioCyci ARA:AT4G27820-MONOMER.

Gene expression databases

Genevestigatori Q9STP4.

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. "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.
    , 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. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 325-506.
    Strain: cv. Columbia.
  4. Cited for: GENE FAMILY, NOMENCLATURE.

Entry informationi

Entry nameiBGL09_ARATH
AccessioniPrimary (citable) accession number: Q9STP4
Secondary accession number(s): Q0WND2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 24, 2009
Last sequence update: November 24, 2009
Last modified: October 1, 2014
This is version 80 of the entry and version 2 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