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Protein

Endo-beta-1,4-glucanase celB

Gene

celB

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
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 4.0. Stable between pH 3.0 and 7.0.1 Publication

Temperature dependencei

Optimum temperature is 45 degrees Celsius. Stable up to 50 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei214NucleophileBy similarity1
Active sitei219Proton donorBy similarity1

GO - Molecular functioni

GO - Biological processi

  • cellulose catabolic process Source: UniProtKB-KW
  • glucan catabolic process Source: ASPGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Protein family/group databases

CAZyiGH7. Glycoside Hydrolase Family 7.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-beta-1,4-glucanase celB (EC:3.2.1.4)
Short name:
Endoglucanase celB
Alternative name(s):
Carboxymethylcellulase celB
Cellulase B
Gene namesi
Name:celB
ORF Names:AO090010000314
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000006564 Componenti: Chromosome 8

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
ChainiPRO_000039515718 – 416Endo-beta-1,4-glucanase celBAdd BLAST399

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi45N-linked (GlcNAc...)Sequence analysis1
Glycosylationi104N-linked (GlcNAc...)Sequence analysis1
Glycosylationi117N-linked (GlcNAc...)Sequence analysis1
Glycosylationi135N-linked (GlcNAc...)Sequence analysis1
Glycosylationi233N-linked (GlcNAc...)Sequence analysis1
Glycosylationi278N-linked (GlcNAc...)Sequence analysis1
Glycosylationi292N-linked (GlcNAc...)Sequence analysis1
Glycosylationi382N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ2TX26.
SMRiQ2TX26.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000182210.
KOiK19357.
OMAiHTNGSEL.
OrthoDBiEOG092C29WB.

Family and domain databases

CDDicd07999. GH7_CBH_EG. 1 hit.
Gene3Di2.70.100.10. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamiPF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSiPR00734. GLHYDRLASE7.
SUPFAMiSSF49899. SSF49899. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q2TX26-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIWTLAPFVA LLPLVTAQQV GTTADAHPRL TTYKCTSQNG CTRQNTSVVL
60 70 80 90 100
DAATHFIHKK GTQTSCTNSN GLDTAICPDK QTCADNCVVD GITDYASYGV
110 120 130 140 150
QTKNDTLTLQ QYLQTGNATK SLSPRVYLLA EDGENYSMLK LLNQEFTFDV
160 170 180 190 200
DASTLVCGMN GALYLSEMEA SGGKSSLNQA GAKYGTGYCD AQCYTTPWIN
210 220 230 240 250
GEGNTESVGS CCQEMDIWEA NARATGLTPH PCNTTGLYEC SGSGCGDSGV
260 270 280 290 300
CDKAGCGFNP YGLGAKDYYG YGLKVNTNET FTVVTQFLTN DNTTSGQLSE
310 320 330 340 350
IRRLYIQNGQ VIQNAAVTSG GKTVDSITKD FCSGEGSAFN RLGGLEEMGH
360 370 380 390 400
ALGRGMVLAL SIWNDAGSFM QWLDGGSAGP CNATEGNPAL IEKLYPDTHV
410
KFSKIRWGDI GSTYRH
Length:416
Mass (Da):44,448
Last modified:January 24, 2006 - v1
Checksum:i437ADE03BF84AB53
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti48V → L in BAA22589 (PubMed:9008887).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D83732 Genomic DNA. Translation: BAA22589.1.
AP007175 Genomic DNA. Translation: BAE66197.1.
RefSeqiXP_001827330.1. XM_001827278.1.

Genome annotation databases

EnsemblFungiiBAE66197; BAE66197; AO090010000314.
GeneIDi5999464.
KEGGiaor:AOR_1_514024.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D83732 Genomic DNA. Translation: BAA22589.1.
AP007175 Genomic DNA. Translation: BAE66197.1.
RefSeqiXP_001827330.1. XM_001827278.1.

3D structure databases

ProteinModelPortaliQ2TX26.
SMRiQ2TX26.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH7. Glycoside Hydrolase Family 7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiBAE66197; BAE66197; AO090010000314.
GeneIDi5999464.
KEGGiaor:AOR_1_514024.

Phylogenomic databases

HOGENOMiHOG000182210.
KOiK19357.
OMAiHTNGSEL.
OrthoDBiEOG092C29WB.

Family and domain databases

CDDicd07999. GH7_CBH_EG. 1 hit.
Gene3Di2.70.100.10. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamiPF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSiPR00734. GLHYDRLASE7.
SUPFAMiSSF49899. SSF49899. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCELB_ASPOR
AccessioniPrimary (citable) accession number: Q2TX26
Secondary accession number(s): O13455
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: January 24, 2006
Last modified: November 30, 2016
This is version 60 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. SIMILARITY comments
    Index of protein domains and families

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.