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Protein

Probable beta-glucosidase K

Gene

bglK

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei232 – 2321By 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.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable beta-glucosidase K (EC:3.2.1.21)
Alternative name(s):
Beta-D-glucoside glucohydrolase K
Cellobiase K
Gentiobiase K
Gene namesi
Name:bglK
ORF Names:AFUA_7G00240
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000002530: Chromosome 7

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 767767Probable beta-glucosidase KPRO_0000394897Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi19 – 191N-linked (GlcNAc...)Sequence Analysis
Glycosylationi324 – 3241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi477 – 4771N-linked (GlcNAc...)Sequence Analysis
Glycosylationi749 – 7491N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ4WA69.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini406 – 541136PA14Add
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 3 family.Curated
Contains 1 PA14 domain.Curated

Phylogenomic databases

eggNOGiCOG1472.
HOGENOMiHOG000031215.
InParanoidiQ4WA69.
KOiK01238.
OMAiQRGGTFF.
OrthoDBiEOG7H799Q.

Family and domain databases

Gene3Di3.20.20.300. 1 hit.
3.40.50.1700. 2 hits.
InterProiIPR026892. Glyco_hydro_3.
IPR019800. Glyco_hydro_3_AS.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
IPR011658. PA14.
[Graphical view]
PANTHERiPTHR30620. PTHR30620. 1 hit.
PfamiPF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
PF07691. PA14. 1 hit.
[Graphical view]
PRINTSiPR00133. GLHYDRLASE3.
SMARTiSM00758. PA14. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 2 hits.
PROSITEiPS00775. GLYCOSYL_HYDROL_F3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q4WA69-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGEICPRRED FDIDYILKNA SLLEKVSLLA GYDFWHTAPL PRFNVPSVRV
60 70 80 90 100
SDGPNGVRGT KFFDGVRAAC LPCGTGLAAT WDQSLLYDAG VLIGQECLAK
110 120 130 140 150
GAHCWLVPTV CIQRSPLGGR GFESFAEDPY ATGKLAAAYI RGAQSTGVIS
160 170 180 190 200
TIKHFAANDQ EHERISVNAV MSERALREVH LLPFQIAIAD SAPGAVMTCY
210 220 230 240 250
NKVNGQHLSE SKEMLDGLLR REWGWKGLIM SDWFGTYSTA EALNAGLGLE
260 270 280 290 300
MPGTTRLRGP LLELAISSRK VSRATLDERA RTVLEFVQRA RKAEVSAVES
310 320 330 340 350
TRDFPEDRRL NRKLAADSIV LLKNESGLLP LNPQTLTSVA LIGPNMKTAA
360 370 380 390 400
FCGGGSASLQ PYYSTSPYQG ITSQLPPGVE VLYETGATSY AFIPELEASE
410 420 430 440 450
VRTPEGQPGL RMRFYRDPPS VQERRVLMGF SNPELDRLFY ADIEAELIAP
460 470 480 490 500
ATGPFQFGLA VYGSASLFLN DQLIIDNTTV QRGGTFFFGK GTLEETATVD
510 520 530 540 550
LVQGQSYQIK VQFASGPSSK LVKPGVVNFG GGAGRLGMVQ VVDPERAIAR
560 570 580 590 600
AVEAAKRADI TILGVGLTRD HESEGFDRSH MDLPPAVASL VTAVLDVAPD
610 620 630 640 650
AILLTQSGTP FSMLPWADLV KTHLHAWFGG NELGNGIADV LFGVVNPSGK
660 670 680 690 700
LPLSFPRRIE DTPTYLNFGS ERGQVTYGEG IYVGYKLLRK SPTSCALSIR
710 720 730 740 750
ARFVVHLLCV LRFDGRHRVR YTECSKLGRR GRSGSSPAVY RGRSNNVVNR
760
TSHQGAQRIS KGGFAAR
Length:767
Mass (Da):83,358
Last modified:July 5, 2005 - v1
Checksum:iBF4924E3FE58BC4E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000015 Genomic DNA. Translation: EAL84867.1.
RefSeqiXP_746905.1. XM_741812.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00001243; CADAFUAP00001243; CADAFUAG00001243.
GeneIDi3504260.
KEGGiafm:AFUA_7G00240.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000015 Genomic DNA. Translation: EAL84867.1.
RefSeqiXP_746905.1. XM_741812.1.

3D structure databases

ProteinModelPortaliQ4WA69.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFUAT00001243; CADAFUAP00001243; CADAFUAG00001243.
GeneIDi3504260.
KEGGiafm:AFUA_7G00240.

Phylogenomic databases

eggNOGiCOG1472.
HOGENOMiHOG000031215.
InParanoidiQ4WA69.
KOiK01238.
OMAiQRGGTFF.
OrthoDBiEOG7H799Q.

Enzyme and pathway databases

UniPathwayiUPA00696.

Family and domain databases

Gene3Di3.20.20.300. 1 hit.
3.40.50.1700. 2 hits.
InterProiIPR026892. Glyco_hydro_3.
IPR019800. Glyco_hydro_3_AS.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
IPR011658. PA14.
[Graphical view]
PANTHERiPTHR30620. PTHR30620. 1 hit.
PfamiPF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
PF07691. PA14. 1 hit.
[Graphical view]
PRINTSiPR00133. GLHYDRLASE3.
SMARTiSM00758. PA14. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 2 hits.
PROSITEiPS00775. GLYCOSYL_HYDROL_F3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
    Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.
    , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
    Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Entry informationi

Entry nameiBGLK_ASPFU
AccessioniPrimary (citable) accession number: Q4WA69
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: July 5, 2005
Last modified: January 7, 2015
This is version 58 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

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.