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Q4WU49

- BGLI_ASPFU

UniProt

Q4WU49 - BGLI_ASPFU

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Protein

Probable beta-glucosidase I

Gene

bglI

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed - 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 sitei225 – 2251By 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 I (EC:3.2.1.21)
Alternative name(s):
Beta-D-glucoside glucohydrolase I
Cellobiase I
Gentiobiase I
Gene namesi
Name:bglI
ORF Names:AFUA_5G07190
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000002530: Chromosome 5

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 838838Probable beta-glucosidase IPRO_0000394886Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi197 – 1971N-linked (GlcNAc...)Sequence Analysis
Glycosylationi493 – 4931N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi5085.CADAFUAP00006281.

Structurei

3D structure databases

ProteinModelPortaliQ4WU49.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini396 – 542147PA14Add
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1472.
HOGENOMiHOG000031215.
InParanoidiQ4WU49.
KOiK05349.
OMAiKTRWRGD.
OrthoDBiEOG7H799Q.

Family and domain databases

Gene3Di3.20.20.300. 1 hit.
3.40.50.1700. 2 hits.
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.
IPR011658. PA14.
[Graphical view]
PANTHERiPTHR30620. PTHR30620. 1 hit.
PfamiPF14310. Fn3-like. 1 hit.
PF00933. 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.

Q4WU49-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVQLDVEKTI EELTLGEKVA LTAGIDFWHT AAVPRLNIPS LRMSDGPNGV
60 70 80 90 100
RGTRFFNGVP AACFPCATAL GATWDTKLLY EVGRLMGEES IAKGAHVVLG
110 120 130 140 150
PTINTQRSPL GGRGFESFAE DGVLSGILAG HYCKGLQETG VAATLKHFVC
160 170 180 190 200
NDQEHERLAV DSIVTMRAMR EIYLLPFQLA MRICKTACVM TAYNKVNGTH
210 220 230 240 250
VSENKQIITD ILRKEWGWDG LVMSDWFGTY STCDAINAGL DLEMPGPTRW
260 270 280 290 300
RGTALAHAVS SNKAFEFVMD ERVRNILNLH NFVEPLGIPE NAPEKALNRP
310 320 330 340 350
EDQALLRRAA AESVVLIKNQ DNILPLKKEK PILVIGPNAK TAAYCGGGSA
360 370 380 390 400
SLDAYYTVTP FEGVAAQSQG EVTFSQGVYS YKELPLLGPL LKTDDGKKGF
410 420 430 440 450
KFRVYNEPPS EPNRQLIDEL HLESSSGFLM DYKHPKIKTF TFYVDMEGYF
460 470 480 490 500
TPEEDGIYDF GVTVVGTGKL FVDDELVVDN SKNQRQGTAM FGNATVEEKG
510 520 530 540 550
SKELKAGQTY KVVLQFGTAP TSDLDMRGVV IFGPGGFRFG AARRVSQEEL
560 570 580 590 600
ISKAAELASQ TSQVVIFAGL TSEWETEGYD RDHMDLPPGS DEMISRVLDA
610 620 630 640 650
NPDTVVVIQS GTPVTMPWAH KAKALLQAWF GGNECGNGIA DVLYGNVNPA
660 670 680 690 700
AKLPLSFPVR LQDNPSYLNF RSERGRVLYG EDIYVGYRYY EKVDLAPLFP
710 720 730 740 750
FGHGLSYTTF SRSDLSLATT PEKPQLEDGE PITVTVSVTN TGSVAGAEIV
760 770 780 790 800
QLWVAPPPTG VNRPVRELKG FTKVFLQPGE TKKVEIVVEK KLATSWWDEQ
810 820 830
REKWASEKGT YEVLVTGTGD EVLKSSFEVE KTRYWLGL
Length:838
Mass (Da):92,208
Last modified:July 5, 2005 - v1
Checksum:i778CBDF5A0B2C14B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000003 Genomic DNA. Translation: EAL91877.1.
RefSeqiXP_753915.1. XM_748822.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00006281; CADAFUAP00006281; CADAFUAG00006281.
GeneIDi3511295.
KEGGiafm:AFUA_5G07190.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000003 Genomic DNA. Translation: EAL91877.1 .
RefSeqi XP_753915.1. XM_748822.1.

3D structure databases

ProteinModelPortali Q4WU49.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5085.CADAFUAP00006281.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADAFUAT00006281 ; CADAFUAP00006281 ; CADAFUAG00006281 .
GeneIDi 3511295.
KEGGi afm:AFUA_5G07190.

Phylogenomic databases

eggNOGi COG1472.
HOGENOMi HOG000031215.
InParanoidi Q4WU49.
KOi K05349.
OMAi KTRWRGD.
OrthoDBi EOG7H799Q.

Enzyme and pathway databases

UniPathwayi UPA00696 .

Family and domain databases

Gene3Di 3.20.20.300. 1 hit.
3.40.50.1700. 2 hits.
InterProi IPR026891. 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.
IPR011658. PA14.
[Graphical view ]
PANTHERi PTHR30620. PTHR30620. 1 hit.
Pfami PF14310. Fn3-like. 1 hit.
PF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
PF07691. PA14. 1 hit.
[Graphical view ]
PRINTSi PR00133. GLHYDRLASE3.
SMARTi SM00758. PA14. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 2 hits.
PROSITEi PS00775. GLYCOSYL_HYDROL_F3. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 nameiBGLI_ASPFU
AccessioniPrimary (citable) accession number: Q4WU49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: July 5, 2005
Last modified: October 29, 2014
This is version 59 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