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Protein

Probable beta-glucosidase A

Gene

bglA

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity).By similarity

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 sitei281By similarity1

GO - Molecular functioni

GO - Biological processi

  • carbohydrate catabolic process Source: ASPGD
  • 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

BRENDAi3.2.1.21. 522.
UniPathwayiUPA00696.

Protein family/group databases

CAZyiGH3. Glycoside Hydrolase Family 3.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable beta-glucosidase A (EC:3.2.1.21)
Alternative name(s):
Beta-D-glucoside glucohydrolase A
Cellobiase A
Gentiobiase A
Gene namesi
Name:bglA
Synonyms:bgl1
ORF Names:AO090009000356
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000006564 Componenti: Chromosome 1

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000039409720 – 861Probable beta-glucosidase AAdd BLAST842

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi62N-linked (GlcNAc...)Sequence analysis1
Glycosylationi212N-linked (GlcNAc...)Sequence analysis1
Glycosylationi253N-linked (GlcNAc...)Sequence analysis1
Glycosylationi316N-linked (GlcNAc...)Sequence analysis1
Glycosylationi323N-linked (GlcNAc...)Sequence analysis1
Glycosylationi355N-linked (GlcNAc...)Sequence analysis1
Glycosylationi443N-linked (GlcNAc...)Sequence analysis1
Glycosylationi524N-linked (GlcNAc...)Sequence analysis1
Glycosylationi543N-linked (GlcNAc...)Sequence analysis1
Glycosylationi565N-linked (GlcNAc...)Sequence analysis1
Glycosylationi669N-linked (GlcNAc...)Sequence analysis1
Glycosylationi713N-linked (GlcNAc...)Sequence analysis1
Glycosylationi846N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Structurei

Secondary structure

1861
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi39 – 41Combined sources3
Helixi42 – 52Combined sources11
Helixi57 – 64Combined sources8
Beta strandi71 – 78Combined sources8
Helixi82 – 84Combined sources3
Beta strandi90 – 92Combined sources3
Helixi110 – 116Combined sources7
Helixi119 – 135Combined sources17
Beta strandi139 – 141Combined sources3
Helixi158 – 160Combined sources3
Helixi166 – 182Combined sources17
Beta strandi186 – 193Combined sources8
Helixi203 – 208Combined sources6
Beta strandi218 – 220Combined sources3
Helixi223 – 228Combined sources6
Helixi232 – 239Combined sources8
Beta strandi243 – 247Combined sources5
Beta strandi249 – 256Combined sources8
Helixi257 – 259Combined sources3
Helixi261 – 264Combined sources4
Helixi265 – 271Combined sources7
Beta strandi276 – 280Combined sources5
Helixi288 – 294Combined sources7
Beta strandi298 – 305Combined sources8
Helixi315 – 322Combined sources8
Helixi328 – 344Combined sources17
Helixi347 – 350Combined sources4
Beta strandi362 – 368Combined sources7
Turni369 – 372Combined sources4
Beta strandi373 – 378Combined sources6
Helixi389 – 399Combined sources11
Beta strandi402 – 408Combined sources7
Beta strandi417 – 423Combined sources7
Helixi424 – 426Combined sources3
Helixi437 – 439Combined sources3
Beta strandi450 – 453Combined sources4
Helixi463 – 472Combined sources10
Turni473 – 475Combined sources3
Beta strandi477 – 481Combined sources5
Helixi487 – 496Combined sources10
Beta strandi498 – 506Combined sources9
Beta strandi518 – 521Combined sources4
Helixi531 – 541Combined sources11
Beta strandi543 – 553Combined sources11
Turni558 – 562Combined sources5
Beta strandi566 – 571Combined sources6
Helixi579 – 587Combined sources9
Beta strandi603 – 605Combined sources3
Helixi606 – 608Combined sources3
Turni617 – 620Combined sources4
Beta strandi624 – 626Combined sources3
Turni628 – 631Combined sources4
Helixi635 – 640Combined sources6
Beta strandi658 – 667Combined sources10
Helixi692 – 695Combined sources4
Beta strandi712 – 715Combined sources4
Helixi717 – 721Combined sources5
Turni724 – 727Combined sources4
Helixi730 – 732Combined sources3
Turni736 – 739Combined sources4
Helixi757 – 760Combined sources4
Beta strandi762 – 772Combined sources11
Beta strandi774 – 776Combined sources3
Beta strandi778 – 780Combined sources3
Beta strandi783 – 787Combined sources5
Beta strandi797 – 801Combined sources5
Beta strandi804 – 806Combined sources3
Beta strandi811 – 819Combined sources9
Helixi820 – 823Combined sources4
Beta strandi825 – 827Combined sources3
Turni828 – 831Combined sources4
Beta strandi832 – 834Combined sources3
Beta strandi841 – 849Combined sources9
Beta strandi853 – 856Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5FJJX-ray1.95A/B/C/D20-861[»]
ProteinModelPortaliQ2UUD6.
SMRiQ2UUD6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 3 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000031215.
KOiK05349.
OMAiAHHSGVG.
OrthoDBiEOG092C0ZJY.

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.

Q2UUD6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLGWIEVAA LAAASVVSAK DDLAYSPPFY PSPWADGQGE WAEVYKRAVD
60 70 80 90 100
IVSQMTLTEK VNLTTGTGWQ LERCVGQTGS VPRLNIPSLC LQDSPLGIRF
110 120 130 140 150
SDYNSAFPAG VNVAATWDKT LAYLRGQAMG EEFSDKGIDV QLGPAAGPLG
160 170 180 190 200
AHPDGGRNWE GFSPDPALTG VLFAETIKGI QDAGVIATAK HYIMNEQEHF
210 220 230 240 250
RQQPEAAGYG FNVSDSLSSN VDDKTMHELY LWPFADAVRA GVGAVMCSYN
260 270 280 290 300
QINNSYGCEN SETLNKLLKA ELGFQGFVMS DWTAHHSGVG AALAGLDMSM
310 320 330 340 350
PGDVTFDSGT SFWGANLTVG VLNGTIPQWR VDDMAVRIMA AYYKVGRDTK
360 370 380 390 400
YTPPNFSSWT RDEYGFAHNH VSEGAYERVN EFVDVQRDHA DLIRRIGAQS
410 420 430 440 450
TVLLKNKGAL PLSRKEKLVA LLGEDAGSNS WGANGCDDRG CDNGTLAMAW
460 470 480 490 500
GSGTANFPYL VTPEQAIQNE VLQGRGNVFA VTDSWALDKI AAAARQASVS
510 520 530 540 550
LVFVNSDSGE GYLSVDGNEG DRNNITLWKN GDNVVKTAAN NCNNTVVIIH
560 570 580 590 600
SVGPVLIDEW YDHPNVTGIL WAGLPGQESG NSIADVLYGR VNPGAKSPFT
610 620 630 640 650
WGKTRESYGS PLVKDANNGN GAPQSDFTQG VFIDYRHFDK FNETPIYEFG
660 670 680 690 700
YGLSYTTFEL SDLHVQPLNA SRYTPTSGMT EAAKNFGEIG DASEYVYPEG
710 720 730 740 750
LERIHEFIYP WINSTDLKAS SDDSNYGWED SKYIPEGATD GSAQPRLPAS
760 770 780 790 800
GGAGGNPGLY EDLFRVSVKV KNTGNVAGDE VPQLYVSLGG PNEPKVVLRK
810 820 830 840 850
FERIHLAPSQ EAVWTTTLTR RDLANWDVSA QDWTVTPYPK TIYVGNSSRK
860
LPLQASLPKA Q
Length:861
Mass (Da):93,415
Last modified:January 24, 2006 - v1
Checksum:i867B9B1DC8301DDA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007150 Genomic DNA. Translation: BAE54829.1.
RefSeqiXP_001816831.1. XM_001816779.2.

Genome annotation databases

EnsemblFungiiBAE54829; BAE54829; AO090009000356.
GeneIDi5988761.
KEGGiaor:AOR_1_586184.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007150 Genomic DNA. Translation: BAE54829.1.
RefSeqiXP_001816831.1. XM_001816779.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5FJJX-ray1.95A/B/C/D20-861[»]
ProteinModelPortaliQ2UUD6.
SMRiQ2UUD6.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH3. Glycoside Hydrolase Family 3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiBAE54829; BAE54829; AO090009000356.
GeneIDi5988761.
KEGGiaor:AOR_1_586184.

Phylogenomic databases

HOGENOMiHOG000031215.
KOiK05349.
OMAiAHHSGVG.
OrthoDBiEOG092C0ZJY.

Enzyme and pathway databases

UniPathwayiUPA00696.
BRENDAi3.2.1.21. 522.

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 nameiBGLA_ASPOR
AccessioniPrimary (citable) accession number: Q2UUD6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: January 24, 2006
Last modified: November 30, 2016
This is version 60 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, Complete proteome, Reference proteome

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.