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P48825

- BGL1_ASPAC

UniProt

P48825 - BGL1_ASPAC

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Protein

Beta-glucosidase 1

Gene
N/A
Organism
Aspergillus aculeatus
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei280 – 2801By similarity

GO - Molecular functioni

  1. beta-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

UniPathwayiUPA00696.

Protein family/group databases

CAZyiGH3. Glycoside Hydrolase Family 3.
mycoCLAPiBGL3A_ASPAC.
BGL3A_ASPSA.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-glucosidase 1 (EC:3.2.1.21)
Alternative name(s):
Beta-D-glucoside glucohydrolase
Cellobiase
Gentiobiase
OrganismiAspergillus aculeatus
Taxonomic identifieri5053 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 860841Beta-glucosidase 1PRO_0000011776Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi61 – 611N-linked (GlcNAc...)Sequence Analysis
Glycosylationi211 – 2111N-linked (GlcNAc...)Sequence Analysis
Glycosylationi252 – 2521N-linked (GlcNAc...)Sequence Analysis
Glycosylationi315 – 3151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi322 – 3221N-linked (GlcNAc...)Sequence Analysis
Glycosylationi354 – 3541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi387 – 3871N-linked (GlcNAc...)Sequence Analysis
Glycosylationi442 – 4421N-linked (GlcNAc...)Sequence Analysis
Glycosylationi523 – 5231N-linked (GlcNAc...)Sequence Analysis
Glycosylationi542 – 5421N-linked (GlcNAc...)Sequence Analysis
Glycosylationi564 – 5641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi658 – 6581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi668 – 6681N-linked (GlcNAc...)Sequence Analysis
Glycosylationi690 – 6901N-linked (GlcNAc...)Sequence Analysis
Glycosylationi712 – 7121N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Structurei

Secondary structure

1
860
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi38 – 403Combined sources
Helixi41 – 5111Combined sources
Helixi56 – 638Combined sources
Beta strandi70 – 778Combined sources
Helixi81 – 833Combined sources
Beta strandi89 – 913Combined sources
Helixi109 – 1157Combined sources
Helixi118 – 13417Combined sources
Beta strandi138 – 1403Combined sources
Helixi157 – 1593Combined sources
Helixi165 – 18117Combined sources
Beta strandi185 – 1928Combined sources
Helixi202 – 2076Combined sources
Beta strandi217 – 2193Combined sources
Helixi222 – 2276Combined sources
Turni228 – 2303Combined sources
Helixi231 – 2388Combined sources
Beta strandi243 – 2464Combined sources
Beta strandi248 – 2514Combined sources
Helixi256 – 2583Combined sources
Helixi260 – 2634Combined sources
Helixi264 – 2707Combined sources
Beta strandi275 – 2795Combined sources
Helixi288 – 2936Combined sources
Beta strandi297 – 3048Combined sources
Helixi314 – 3218Combined sources
Helixi327 – 34317Combined sources
Helixi346 – 3483Combined sources
Beta strandi362 – 3676Combined sources
Turni368 – 3714Combined sources
Beta strandi372 – 3776Combined sources
Turni386 – 3883Combined sources
Helixi389 – 39810Combined sources
Beta strandi401 – 4077Combined sources
Beta strandi416 – 4227Combined sources
Helixi423 – 4253Combined sources
Helixi436 – 4383Combined sources
Beta strandi449 – 4524Combined sources
Helixi462 – 47211Combined sources
Beta strandi476 – 4805Combined sources
Helixi486 – 49510Combined sources
Beta strandi497 – 5059Combined sources
Beta strandi517 – 5204Combined sources
Helixi530 – 54011Combined sources
Beta strandi542 – 55211Combined sources
Turni557 – 5615Combined sources
Beta strandi565 – 5706Combined sources
Helixi575 – 5773Combined sources
Helixi578 – 5869Combined sources
Beta strandi602 – 6043Combined sources
Helixi605 – 6073Combined sources
Beta strandi623 – 6253Combined sources
Turni627 – 6304Combined sources
Helixi634 – 6396Combined sources
Beta strandi657 – 66610Combined sources
Helixi691 – 6944Combined sources
Beta strandi711 – 7144Combined sources
Helixi716 – 7205Combined sources
Turni723 – 7264Combined sources
Helixi729 – 7324Combined sources
Turni735 – 7384Combined sources
Beta strandi750 – 7545Combined sources
Helixi756 – 7594Combined sources
Beta strandi761 – 77111Combined sources
Beta strandi773 – 7753Combined sources
Beta strandi777 – 7793Combined sources
Beta strandi782 – 7865Combined sources
Beta strandi796 – 8005Combined sources
Beta strandi803 – 8053Combined sources
Beta strandi810 – 8189Combined sources
Helixi819 – 8224Combined sources
Beta strandi824 – 8263Combined sources
Turni827 – 8304Combined sources
Beta strandi831 – 8333Combined sources
Beta strandi840 – 8467Combined sources
Beta strandi852 – 8554Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IIBX-ray1.80A/B20-860[»]
4IICX-ray1.90A/B20-860[»]
4IIDX-ray2.30A/B20-860[»]
4IIEX-ray2.00A/B20-860[»]
4IIFX-ray2.45A/B20-860[»]
4IIGX-ray2.30A/B20-860[»]
4IIHX-ray2.00A/B20-860[»]
ProteinModelPortaliP48825.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 3 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.300. 1 hit.
3.40.50.1700. 1 hit.
InterProiIPR026891. Fn3-like.
IPR026892. Glyco_hydro_3.
IPR019800. Glyco_hydro_3_AS.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR30620. PTHR30620. 1 hit.
PfamiPF14310. Fn3-like. 1 hit.
PF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
[Graphical view]
PRINTSiPR00133. GLHYDRLASE3.
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 2 hits.
PROSITEiPS00775. GLYCOSYL_HYDROL_F3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P48825-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLSWLEAAA LTAASVVSAD ELAFSPPFYP SPWANGQGEW AEAYQRAVAI
60 70 80 90 100
VSQMTLDEKV NLTTGTGWEL EKCVGQTGGV PRLNIGGMCL QDSPLGIRDS
110 120 130 140 150
DYNSAFPAGV NVAATWDKNL AYLRGQAMGQ EFSDKGIDVQ LGPAAGPLGR
160 170 180 190 200
SPDGGRNWEG FSPDPALTGV LFAETIKGIQ DAGVVATAKH YILNEQEHFR
210 220 230 240 250
QVAEAAGYGF NISDTISSNV DDKTIHEMYL WPFADAVRAG VGAIMCSYNQ
260 270 280 290 300
INNSYGCQNS YTLNKLLKAE LGFQGFVMSD WGAHHSGVGS ALAGLDMSMP
310 320 330 340 350
GDITFDSATS FWGTNLTIAV LNGTVPQWRV DDMAVRIMAA YYKVGRDRLY
360 370 380 390 400
QPPNFSSWTR DEYGFKYFYP QEGPYEKVNH FVNVQRNHSE VIRKLGADST
410 420 430 440 450
VLLKNNNALP LTGKERKVAI LGEDAGSNSY GANGCSDRGC DNGTLAMAWG
460 470 480 490 500
SGTAEFPYLV TPEQAIQAEV LKHKGSVYAI TDNWALSQVE TLAKQASVSL
510 520 530 540 550
VFVNSDAGEG YISVDGNEGD RNNLTLWKNG DNLIKAAANN CNNTIVVIHS
560 570 580 590 600
VGPVLVDEWY DHPNVTAILW AGLPGQESGN SLADVLYGRV NPGAKSPFTW
610 620 630 640 650
GKTREAYGDY LVRELNNGNG APQDDFSEGV FIDYRGFDKR NETPIYEFGH
660 670 680 690 700
GLSYTTFNYS GLHIQVLNAS SNAQVATETG AAPTFGQVGN ASDYVYPEGL
710 720 730 740 750
TRISKFIYPW LNSTDLKASS GDPYYGVDTA EHVPEGATDG SPQPVLPAGG
760 770 780 790 800
GSGGNPRLYD ELIRVSVTVK NTGRVAGDAV PQLYVSLGGP NEPKVVLRKF
810 820 830 840 850
DRLTLKPSEE TVWTTTLTRR DLSNWDVAAQ DWVITSYPKK VHVGSSSRQL
860
PLHAALPKVQ
Length:860
Mass (Da):93,053
Last modified:February 1, 1996 - v1
Checksum:i4B484778B00FC694
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D64088 mRNA. Translation: BAA10968.1.
PIRiJC4939.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D64088 mRNA. Translation: BAA10968.1 .
PIRi JC4939.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4IIB X-ray 1.80 A/B 20-860 [» ]
4IIC X-ray 1.90 A/B 20-860 [» ]
4IID X-ray 2.30 A/B 20-860 [» ]
4IIE X-ray 2.00 A/B 20-860 [» ]
4IIF X-ray 2.45 A/B 20-860 [» ]
4IIG X-ray 2.30 A/B 20-860 [» ]
4IIH X-ray 2.00 A/B 20-860 [» ]
ProteinModelPortali P48825.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P48825.
ChEMBLi CHEMBL3493.

Protein family/group databases

CAZyi GH3. Glycoside Hydrolase Family 3.
mycoCLAPi BGL3A_ASPAC.
BGL3A_ASPSA.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00696 .

Family and domain databases

Gene3Di 3.20.20.300. 1 hit.
3.40.50.1700. 1 hit.
InterProi IPR026891. Fn3-like.
IPR026892. Glyco_hydro_3.
IPR019800. Glyco_hydro_3_AS.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
PANTHERi PTHR30620. PTHR30620. 1 hit.
Pfami PF14310. Fn3-like. 1 hit.
PF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
[Graphical view ]
PRINTSi PR00133. GLHYDRLASE3.
SUPFAMi SSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 2 hits.
PROSITEi PS00775. GLYCOSYL_HYDROL_F3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning and sequencing of the cDNA encoding beta-glucosidase 1 from Aspergillus aculeatus."
    Kawaguchi T., Enoki T., Tsurumaki S., Sumitani J., Ueda M., Ooi T., Arai M.
    Gene 173:287-288(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: F-50.

Entry informationi

Entry nameiBGL1_ASPAC
AccessioniPrimary (citable) accession number: P48825
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: October 29, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3