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Q4WLY1

- BGLJ_ASPFU

UniProt

Q4WLY1 - BGLJ_ASPFU

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Protein

Probable beta-glucosidase J

Gene

bglJ

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 sitei233 – 2331By 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 J (EC:3.2.1.21)
Alternative name(s):
Beta-D-glucoside glucohydrolase J
Cellobiase J
Gentiobiase J
Gene namesi
Name:bglJ
ORF Names:AFUA_6G11910
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000002530: Chromosome 6

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 – 865865Probable beta-glucosidase JPRO_0000394893Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi330 – 3301N-linked (GlcNAc...)Sequence Analysis
Glycosylationi447 – 4471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi503 – 5031N-linked (GlcNAc...)Sequence Analysis
Glycosylationi764 – 7641N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi5085.CADAFUAP00001941.

Structurei

3D structure databases

ProteinModelPortaliQ4WLY1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini415 – 548134PA14Add
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1472.
HOGENOMiHOG000031215.
InParanoidiQ4WLY1.
KOiK05349.
OrthoDBiEOG7H799Q.

Family and domain databases

Gene3Di3.20.20.300. 1 hit.
3.40.50.1700. 2 hits.
InterProiIPR026891. Fn3-like.
IPR026892. Glyco_hydro_3.
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.

Sequencei

Sequence statusi: Complete.

Q4WLY1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGSIDTVGMG QRAIDQIISE LSLNEKVALL SGVDAWHTFA IPRLGIPSIR
60 70 80 90 100
TTDGPNGARG TRYFNGVPSA CLPCGTALGA TFDRDLIFSL GQLLAAECRA
110 120 130 140 150
KGAHVLLGPT INIQRGPLGG RGFESFSEDP VLSGLAAASY CSGVQDGGVV
160 170 180 190 200
PTLKHLVCND QEHERVAVSA LVTPRALREI YLLPFQLAIQ GARPGAVMTS
210 220 230 240 250
YNKVNGLHAS ENPGLIRDIL RGEWGYEGAV ISDWFGTYSV ADAVNAGLDL
260 270 280 290 300
EMPGPTRFRG PALMHALTSN KVSEKTLNER VRKVLELVQL ASRAGVPEYA
310 320 330 340 350
PERKLNRPED RALLRRAAGE SVVLLKNDKN DSTNSPILPL DREKTTLVIG
360 370 380 390 400
PNADLAAYCG GGSASLLAYY TVTPRQGIAD KCGAEQVVFS QGCYGHKELP
410 420 430 440 450
LLGEHLRTIE TGQPGYTFRV YTEPPPASGS FKGSDSRTPV DELHMTNSSA
460 470 480 490 500
FLMDYSHPQI SGDTYYATLE GTFEPPESGV YEFGLTVAGT GLLYIDGVLV
510 520 530 540 550
VDNKTVQRAG TSFFGIGTVE ERGERYLEAG KKHHVFVEFG TAPTSNLQHH
560 570 580 590 600
HGVVSFGPGG LRLGGCRKLD TDTAIQQAVQ SAAQADQVVV CVGLSGDWES
610 620 630 640 650
EGFDRPHMDL PPGTDELVNA VLAVQPNAVI VVQSGTPVTM PWADKAKALL
660 670 680 690 700
QAWYGGNEAG NGIADVLFGD VNPSAKLPLT FPRELAQNPS YLSYRSERGR
710 720 730 740 750
VLYSEDIYVG YRYYDTTGQP PLFRFGHGLS YSTFHLRDLT VRETAPYAAN
760 770 780 790 800
IKESSLRVSV TVSNTSARPG AEVVLVYVRP PAAACSVGRP VRELKGYEKV
810 820 830 840 850
MLQPGETREV SITIPLGLAT SFWDEGCDAW LSEKGLYFVE AVGTGEGNTL
860
VAPLTVQVSR VWNGL
Length:865
Mass (Da):92,992
Last modified:June 15, 2010 - v2
Checksum:i3D9E8E3E09B04762
GO

Sequence cautioni

The sequence EAL89033.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AAHF01000006 Genomic DNA. Translation: EAL89033.1. Sequence problems.
RefSeqiXP_751071.1. XM_745978.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00001941; CADAFUAP00001941; CADAFUAG00001941.
GeneIDi3508376.
KEGGiafm:AFUA_6G11910.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AAHF01000006 Genomic DNA. Translation: EAL89033.1 . Sequence problems.
RefSeqi XP_751071.1. XM_745978.1.

3D structure databases

ProteinModelPortali Q4WLY1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5085.CADAFUAP00001941.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADAFUAT00001941 ; CADAFUAP00001941 ; CADAFUAG00001941 .
GeneIDi 3508376.
KEGGi afm:AFUA_6G11910.

Phylogenomic databases

eggNOGi COG1472.
HOGENOMi HOG000031215.
InParanoidi Q4WLY1.
KOi K05349.
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.
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.
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 nameiBGLJ_ASPFU
AccessioniPrimary (citable) accession number: Q4WLY1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: October 29, 2014
This is version 60 of the entry and version 2 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