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Protein

Endo-beta-1,4-glucanase B

Gene

eglB

Organism
Aspergillus niger
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. Involved in the degradation of complex natural cellulosic substrates.1 Publication

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

pH dependencei

Optimum pH is 6.0.1 Publication

Temperature dependencei

Optimum temperature is 70 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei160Proton donorBy similarity1
Active sitei266NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.
mycoCLAPiEGL5B_ASPNG.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-beta-1,4-glucanase B (EC:3.2.1.4)
Short name:
Endoglucanase B
Alternative name(s):
Carboxymethylcellulase B
Cellulase B
Gene namesi
Name:eglB
Synonyms:eng1
OrganismiAspergillus niger
Taxonomic identifieri5061 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_500006505219 – 331Endo-beta-1,4-glucanase BAdd BLAST313

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi38N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi100N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi211N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi288N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiO74706.

Expressioni

Inductioni

Expression is under the control of the xylanolytic transcriptional activator xlnR.1 Publication

Structurei

Secondary structure

1331
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi32 – 39Combined sources8
Beta strandi45 – 49Combined sources5
Turni52 – 54Combined sources3
Helixi61 – 69Combined sources9
Beta strandi74 – 79Combined sources6
Helixi81 – 84Combined sources4
Helixi95 – 110Combined sources16
Beta strandi114 – 119Combined sources6
Helixi133 – 147Combined sources15
Beta strandi153 – 156Combined sources4
Helixi166 – 182Combined sources17
Beta strandi189 – 192Combined sources4
Turni194 – 197Combined sources4
Turni199 – 201Combined sources3
Helixi202 – 205Combined sources4
Helixi207 – 211Combined sources5
Beta strandi219 – 226Combined sources8
Beta strandi231 – 233Combined sources3
Helixi243 – 258Combined sources16
Beta strandi262 – 268Combined sources7
Helixi273 – 287Combined sources15
Turni290 – 292Combined sources3
Beta strandi293 – 301Combined sources9
Turni314 – 316Combined sources3
Helixi318 – 327Combined sources10
Helixi328 – 330Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5I77X-ray1.80A31-330[»]
5I78X-ray1.58A/B31-330[»]
5I79X-ray2.35A/B31-330[»]
ProteinModelPortaliO74706.
SMRiO74706.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IHV9. Eukaryota.
COG2730. LUCA.

Family and domain databases

InterProiView protein in InterPro
IPR001547. Glyco_hydro_5.
IPR017853. Glycoside_hydrolase_SF.
PfamiView protein in Pfam
PF00150. Cellulase. 1 hit.
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

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

O74706-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFQSTLLLA AAAGSALAVP HGSGHKKRAS VFEWFGSNES GAEFGTNIPG
60 70 80 90 100
VWGTDYIFPD PSTISTLIGK GMNFFRVQFM MERLLPDSMT GSYDEEYLAN
110 120 130 140 150
LTTVVKAVTD GGAHALIDPH NYGRYNGEII SSTSDFQTFW QNLAGQYKDN
160 170 180 190 200
DLVMFDTNNE YYDMDQDLVL NLNQAAINGI RAAGASQYIF VEGNSWTGAW
210 220 230 240 250
TWVDVNDNMK NLTDPEDKIV YEMHQYLDSD GSGTSETCVS GTIGKERITD
260 270 280 290 300
ATQWLKDNKK VGFIGEYAGG SNDVCRSAVS GMLEYMANNT DVWKGASWWA
310 320 330
AGPWWGDYIF SLEPPDGTAY TGMLDILETY L
Length:331
Mass (Da):36,559
Last modified:November 1, 1998 - v1
Checksum:iF3AE4BF70007C707
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti13A → G in AAG50051 (PubMed:16233124).Curated1
Sequence conflicti23S → P in AAG50051 (PubMed:16233124).Curated1
Sequence conflicti63T → A in AAG50051 (PubMed:16233124).Curated1
Sequence conflicti69G → D in AAG50051 (PubMed:16233124).Curated1
Sequence conflicti105V → I in AAG50051 (PubMed:16233124).Curated1
Sequence conflicti117I → V in AAG50051 (PubMed:16233124).Curated1
Sequence conflicti141Q → E in AAG50051 (PubMed:16233124).Curated1
Sequence conflicti162Y → H in AAG50051 (PubMed:16233124).Curated1
Sequence conflicti185A → AT in AAG50051 (PubMed:16233124).Curated1
Sequence conflicti241G → E in AAG50051 (PubMed:16233124).Curated1
Sequence conflicti248 – 250ITD → VTE in AAG50051 (PubMed:16233124).Curated3
Sequence conflicti329T → A in AAG50051 (PubMed:16233124).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GQ292753 Genomic DNA. Translation: ACT68011.1.
AF331518 mRNA. Translation: AAG50051.1.
AJ224452 Genomic DNA. Translation: CAA11965.1.

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.

Entry informationi

Entry nameiEGLB_ASPNG
AccessioniPrimary (citable) accession number: O74706
Secondary accession number(s): Q9C3Z7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: November 1, 1998
Last modified: July 5, 2017
This is version 81 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families