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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei281 – 2811By similarity

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.

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

Organism-specific databases

EuPathDBiFungiDB:AO090009000356.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 861842Probable beta-glucosidase APRO_0000394097Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi62 – 621N-linked (GlcNAc...)Sequence analysis
Glycosylationi212 – 2121N-linked (GlcNAc...)Sequence analysis
Glycosylationi253 – 2531N-linked (GlcNAc...)Sequence analysis
Glycosylationi316 – 3161N-linked (GlcNAc...)Sequence analysis
Glycosylationi323 – 3231N-linked (GlcNAc...)Sequence analysis
Glycosylationi355 – 3551N-linked (GlcNAc...)Sequence analysis
Glycosylationi443 – 4431N-linked (GlcNAc...)Sequence analysis
Glycosylationi524 – 5241N-linked (GlcNAc...)Sequence analysis
Glycosylationi543 – 5431N-linked (GlcNAc...)Sequence analysis
Glycosylationi565 – 5651N-linked (GlcNAc...)Sequence analysis
Glycosylationi669 – 6691N-linked (GlcNAc...)Sequence analysis
Glycosylationi713 – 7131N-linked (GlcNAc...)Sequence analysis
Glycosylationi846 – 8461N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Structurei

Secondary structure

1
861
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi39 – 413Combined sources
Helixi42 – 5211Combined sources
Helixi57 – 648Combined sources
Beta strandi71 – 788Combined sources
Helixi82 – 843Combined sources
Beta strandi90 – 923Combined sources
Helixi110 – 1167Combined sources
Helixi119 – 13517Combined sources
Beta strandi139 – 1413Combined sources
Helixi158 – 1603Combined sources
Helixi166 – 18217Combined sources
Beta strandi186 – 1938Combined sources
Helixi203 – 2086Combined sources
Beta strandi218 – 2203Combined sources
Helixi223 – 2286Combined sources
Helixi232 – 2398Combined sources
Beta strandi243 – 2475Combined sources
Beta strandi249 – 2568Combined sources
Helixi257 – 2593Combined sources
Helixi261 – 2644Combined sources
Helixi265 – 2717Combined sources
Beta strandi276 – 2805Combined sources
Helixi288 – 2947Combined sources
Beta strandi298 – 3058Combined sources
Helixi315 – 3228Combined sources
Helixi328 – 34417Combined sources
Helixi347 – 3504Combined sources
Beta strandi362 – 3687Combined sources
Turni369 – 3724Combined sources
Beta strandi373 – 3786Combined sources
Helixi389 – 39911Combined sources
Beta strandi402 – 4087Combined sources
Beta strandi417 – 4237Combined sources
Helixi424 – 4263Combined sources
Helixi437 – 4393Combined sources
Beta strandi450 – 4534Combined sources
Helixi463 – 47210Combined sources
Turni473 – 4753Combined sources
Beta strandi477 – 4815Combined sources
Helixi487 – 49610Combined sources
Beta strandi498 – 5069Combined sources
Beta strandi518 – 5214Combined sources
Helixi531 – 54111Combined sources
Beta strandi543 – 55311Combined sources
Turni558 – 5625Combined sources
Beta strandi566 – 5716Combined sources
Helixi579 – 5879Combined sources
Beta strandi603 – 6053Combined sources
Helixi606 – 6083Combined sources
Turni617 – 6204Combined sources
Beta strandi624 – 6263Combined sources
Turni628 – 6314Combined sources
Helixi635 – 6406Combined sources
Beta strandi658 – 66710Combined sources
Helixi692 – 6954Combined sources
Beta strandi712 – 7154Combined sources
Helixi717 – 7215Combined sources
Turni724 – 7274Combined sources
Helixi730 – 7323Combined sources
Turni736 – 7394Combined sources
Helixi757 – 7604Combined sources
Beta strandi762 – 77211Combined sources
Beta strandi774 – 7763Combined sources
Beta strandi778 – 7803Combined sources
Beta strandi783 – 7875Combined sources
Beta strandi797 – 8015Combined sources
Beta strandi804 – 8063Combined sources
Beta strandi811 – 8199Combined sources
Helixi820 – 8234Combined sources
Beta strandi825 – 8273Combined sources
Turni828 – 8314Combined sources
Beta strandi832 – 8343Combined sources
Beta strandi841 – 8499Combined sources
Beta strandi853 – 8564Combined sources

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 3 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000031215.
KOiK05349.
OMAiAHHSGVG.
OrthoDBiEOG7HMS8F.

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

EnsemblFungiiCADAORAT00003820; CADAORAP00003752; CADAORAG00003820.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
5FJJX-ray1.95A/B/C/D20-861[»]
ProteinModelPortaliQ2UUD6.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAORAT00003820; CADAORAP00003752; CADAORAG00003820.
GeneIDi5988761.
KEGGiaor:AOR_1_586184.

Organism-specific databases

EuPathDBiFungiDB:AO090009000356.

Phylogenomic databases

HOGENOMiHOG000031215.
KOiK05349.
OMAiAHHSGVG.
OrthoDBiEOG7HMS8F.

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...

Publicationsi

  1. "Genome sequencing and analysis of Aspergillus oryzae."
    Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.
    , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
    Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 42149 / RIB 40.

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: July 6, 2016
This is version 57 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.