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Protein

Beta-glucosidase 1

Gene
N/A
Organism
Aspergillus aculeatus
Status
Reviewed-Annotation score: Annotation score: 3 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: cellulose degradation

This protein is involved in the pathway cellulose degradation, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway cellulose degradation and in Glycan metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei280By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

BRENDAi3.2.1.21. 488.
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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3493.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000001177620 – 860Beta-glucosidase 1Add BLAST841

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi61N-linked (GlcNAc...)Sequence analysis1
Glycosylationi211N-linked (GlcNAc...)Sequence analysis1
Glycosylationi252N-linked (GlcNAc...)Sequence analysis1
Glycosylationi315N-linked (GlcNAc...)Sequence analysis1
Glycosylationi322N-linked (GlcNAc...)Sequence analysis1
Glycosylationi354N-linked (GlcNAc...)Sequence analysis1
Glycosylationi387N-linked (GlcNAc...)Sequence analysis1
Glycosylationi442N-linked (GlcNAc...)Sequence analysis1
Glycosylationi523N-linked (GlcNAc...)Sequence analysis1
Glycosylationi542N-linked (GlcNAc...)Sequence analysis1
Glycosylationi564N-linked (GlcNAc...)Sequence analysis1
Glycosylationi658N-linked (GlcNAc...)Sequence analysis1
Glycosylationi668N-linked (GlcNAc...)Sequence analysis1
Glycosylationi690N-linked (GlcNAc...)Sequence analysis1
Glycosylationi712N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiP48825.

Interactioni

Chemistry databases

BindingDBiP48825.

Structurei

Secondary structure

1860
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi38 – 40Combined sources3
Helixi41 – 51Combined sources11
Helixi56 – 63Combined sources8
Beta strandi70 – 77Combined sources8
Helixi81 – 83Combined sources3
Beta strandi89 – 91Combined sources3
Helixi109 – 115Combined sources7
Helixi118 – 134Combined sources17
Beta strandi138 – 140Combined sources3
Helixi157 – 159Combined sources3
Helixi165 – 181Combined sources17
Beta strandi185 – 192Combined sources8
Helixi202 – 207Combined sources6
Beta strandi217 – 219Combined sources3
Helixi222 – 227Combined sources6
Turni228 – 230Combined sources3
Helixi231 – 238Combined sources8
Beta strandi243 – 246Combined sources4
Beta strandi248 – 251Combined sources4
Helixi256 – 258Combined sources3
Helixi260 – 263Combined sources4
Helixi264 – 270Combined sources7
Beta strandi275 – 279Combined sources5
Helixi288 – 293Combined sources6
Beta strandi297 – 304Combined sources8
Helixi314 – 321Combined sources8
Helixi327 – 343Combined sources17
Helixi346 – 348Combined sources3
Beta strandi362 – 367Combined sources6
Turni368 – 371Combined sources4
Beta strandi372 – 377Combined sources6
Turni386 – 388Combined sources3
Helixi389 – 398Combined sources10
Beta strandi401 – 407Combined sources7
Beta strandi416 – 422Combined sources7
Helixi423 – 425Combined sources3
Helixi436 – 438Combined sources3
Beta strandi449 – 452Combined sources4
Helixi462 – 472Combined sources11
Beta strandi476 – 480Combined sources5
Helixi486 – 495Combined sources10
Beta strandi497 – 505Combined sources9
Beta strandi517 – 520Combined sources4
Helixi530 – 540Combined sources11
Beta strandi542 – 552Combined sources11
Turni557 – 561Combined sources5
Beta strandi565 – 570Combined sources6
Helixi575 – 577Combined sources3
Helixi578 – 586Combined sources9
Beta strandi602 – 604Combined sources3
Helixi605 – 607Combined sources3
Beta strandi623 – 625Combined sources3
Turni627 – 630Combined sources4
Helixi634 – 639Combined sources6
Beta strandi657 – 666Combined sources10
Helixi691 – 694Combined sources4
Beta strandi711 – 714Combined sources4
Helixi716 – 720Combined sources5
Turni723 – 726Combined sources4
Helixi729 – 732Combined sources4
Turni735 – 738Combined sources4
Beta strandi750 – 754Combined sources5
Helixi756 – 759Combined sources4
Beta strandi761 – 771Combined sources11
Beta strandi773 – 775Combined sources3
Beta strandi777 – 779Combined sources3
Beta strandi782 – 786Combined sources5
Beta strandi796 – 800Combined sources5
Beta strandi803 – 805Combined sources3
Beta strandi810 – 818Combined sources9
Helixi819 – 822Combined sources4
Beta strandi824 – 826Combined sources3
Turni827 – 830Combined sources4
Beta strandi831 – 833Combined sources3
Beta strandi840 – 846Combined sources7
Beta strandi852 – 855Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
SMRiP48825.
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. 4 hits.
PfamiPF14310. Fn3-like. 1 hit.
PF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
[Graphical view]
PRINTSiPR00133. GLHYDRLASE3.
SMARTiSM01217. Fn3_like. 1 hit.
[Graphical view]
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:
EMBLi
GenBanki
DDBJi
Links Updated
D64088 mRNA. Translation: BAA10968.1.
PIRiJC4939.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D64088 mRNA. Translation: BAA10968.1.
PIRiJC4939.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
SMRiP48825.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP48825.
ChEMBLiCHEMBL3493.

Protein family/group databases

CAZyiGH3. Glycoside Hydrolase Family 3.
mycoCLAPiBGL3A_ASPAC.
BGL3A_ASPSA.

Proteomic databases

PRIDEiP48825.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00696.
BRENDAi3.2.1.21. 488.

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. 4 hits.
PfamiPF14310. Fn3-like. 1 hit.
PF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
[Graphical view]
PRINTSiPR00133. GLHYDRLASE3.
SMARTiSM01217. Fn3_like. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 2 hits.
PROSITEiPS00775. GLYCOSYL_HYDROL_F3. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 71 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.