Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Probable beta-glucosidase M

Gene

bglM

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 sitei290 – 2901By similarity

GO - Molecular functioni

  1. beta-galactosidase activity Source: ASPGD
  2. 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 M (EC:3.2.1.21)
Alternative name(s):
Beta-D-glucoside glucohydrolase M
Cellobiase M
Gentiobiase M
Gene namesi
Name:bglM
ORF Names:AFUA_1G17410
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000002530: Chromosome 1

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
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 769747Probable beta-glucosidase MPRO_0000394906Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi28 – 281N-linked (GlcNAc...)Sequence Analysis
Glycosylationi75 – 751N-linked (GlcNAc...)Sequence Analysis
Glycosylationi262 – 2621N-linked (GlcNAc...)Sequence Analysis
Glycosylationi318 – 3181N-linked (GlcNAc...)Sequence Analysis
Glycosylationi325 – 3251N-linked (GlcNAc...)Sequence Analysis
Glycosylationi396 – 3961N-linked (GlcNAc...)Sequence Analysis
Glycosylationi437 – 4371N-linked (GlcNAc...)Sequence Analysis
Glycosylationi510 – 5101N-linked (GlcNAc...)Sequence Analysis
Glycosylationi546 – 5461N-linked (GlcNAc...)Sequence Analysis
Glycosylationi625 – 6251N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi5085.CADAFUAP00007078.

Structurei

3D structure databases

ProteinModelPortaliQ4WR62.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 3 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG1472.
HOGENOMiHOG000031215.
InParanoidiQ4WR62.
KOiK05349.
OMAiNITPQFE.
OrthoDBiEOG7HMS8F.

Family and domain databases

Gene3Di3.20.20.300. 1 hit.
3.40.50.1700. 1 hit.
InterProiIPR026891. Fn3-like.
IPR026892. Glyco_hydro_3.
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.

Sequencei

Sequence statusi: Complete.

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

Q4WR62-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHSNVGLAGL AGLLATASVC LSAPADQNIT SDTYFYGQSP PVYPSPEGTG
60 70 80 90 100
TGSWAAAYAK AKKFVAQLTP EEKVNLTAGT DANNGCSGNI AAIPRLNFPG
110 120 130 140 150
LCVSDAGNGL RGTDYVSSWP SGLHVGASWN KALARQRAVQ MATEFRKKGV
160 170 180 190 200
NVLLGPVVGP LGRVAEAGRN WEGFSNDPYL SGALVYETVD GAQSVGVATC
210 220 230 240 250
TKHYILNEQE TNRNPGMEDG VEVAAVSSNI DDKTMHELYL WPFQDAVLAG
260 270 280 290 300
SASIMCSYNR VNNSYGCQNS KTLNGLLKTE LGFQGYVMTD WGAQHAGIAG
310 320 330 340 350
ANAGLDMVMP STETWGANLT TAISNGTMDA SRLDDMATRI IASWYQMNQD
360 370 380 390 400
SDFPSPGAGM PSDMYAPHQR VIGRDASSKQ TLLRGAIEGH VLVKNNHSAL
410 420 430 440 450
PLKSPQLLSV FGYDAKGPNA LKQNFNWLSY SPAIQENHTL WVGGGSGANN
460 470 480 490 500
AAYIDAPIDA IQRQAYEDGT SVLYDISSED PEVDPTTDAC LVFINSYATE
510 520 530 540 550
GWDRPGLADN SSDTLVKNVA RKCANTIVTI HNAGIRVVGE WIDHENVTAV
560 570 580 590 600
IFAHLPGQDS GRALVELLYG RANPSGKLPY TVAKKVEDYG SLLHPSLPET
610 620 630 640 650
PYGLFPQSDF DEGVYIDYRA FDRANITAQF EFGFGLSYTS FDYSGLQISN
660 670 680 690 700
PKQSPQYPPS AAIQQGGNPH LWDNIVTVSA EIKNTGRVAG AEVAQLYIGI
710 720 730 740 750
PNGPVRQLRG FEKVDVSAGE TTQVQFALNR RDLSTWDVEA QQWSLQRGTY
760
RVYVGRSSRD LPLTGSFTL
Length:769
Mass (Da):82,681
Last modified:July 5, 2005 - v1
Checksum:i79C92A56D4325D19
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000004 Genomic DNA. Translation: EAL91070.1.
RefSeqiXP_753108.1. XM_748015.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00007078; CADAFUAP00007078; CADAFUAG00007078.
GeneIDi3510140.
KEGGiafm:AFUA_1G17410.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000004 Genomic DNA. Translation: EAL91070.1.
RefSeqiXP_753108.1. XM_748015.1.

3D structure databases

ProteinModelPortaliQ4WR62.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5085.CADAFUAP00007078.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFUAT00007078; CADAFUAP00007078; CADAFUAG00007078.
GeneIDi3510140.
KEGGiafm:AFUA_1G17410.

Phylogenomic databases

eggNOGiCOG1472.
HOGENOMiHOG000031215.
InParanoidiQ4WR62.
KOiK05349.
OMAiNITPQFE.
OrthoDBiEOG7HMS8F.

Enzyme and pathway databases

UniPathwayiUPA00696.

Family and domain databases

Gene3Di3.20.20.300. 1 hit.
3.40.50.1700. 1 hit.
InterProiIPR026891. Fn3-like.
IPR026892. Glyco_hydro_3.
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.
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 nameiBGLM_ASPFU
AccessioniPrimary (citable) accession number: Q4WR62
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: July 5, 2005
Last modified: January 7, 2015
This is version 55 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.