Endo-beta-1,4-glucanase celB precursor - Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)

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Q2TX26 (CELB_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 35. History...

Clusters with 100%, 90%, 50% identity |

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Endo-beta-1,4-glucanase celB
Short name=Endoglucanase celB
EC=3.2.1.4

Alternative name(s):
Carboxymethylcellulase celB
Cellulase B

Gene names

Name:	celB
ORF Names:	AO090010000314

Organism

Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]

Taxonomic identifier

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	416 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1
Catalytic activity	Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Subcellular location	Secreted By similarity.
Sequence similarities	Belongs to the glycosyl hydrolase 7 (cellulase C) family.
Biophysicochemical properties	pH dependence: Optimum pH is 4.0. Stable between pH 3.0 and 7.0. Ref.1 Temperature dependence: Optimum temperature is 45 degrees Celsius. Stable up to 50 degrees Celsius.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cellulase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

17

Potential

Chain

399

Endo-beta-1,4-glucanase celB

PRO_0000395157

Sites

Active site

1

Nucleophile By similarity

Active site

1

Proton donor By similarity

Amino acid modifications

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

1

V → L in BAA22589. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q2TX26 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 437ADE03BF84AB53
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416

44,448

        10         20         30         40         50         60 
MIWTLAPFVA LLPLVTAQQV GTTADAHPRL TTYKCTSQNG CTRQNTSVVL DAATHFIHKK 

        70         80         90        100        110        120 
GTQTSCTNSN GLDTAICPDK QTCADNCVVD GITDYASYGV QTKNDTLTLQ QYLQTGNATK 

       130        140        150        160        170        180 
SLSPRVYLLA EDGENYSMLK LLNQEFTFDV DASTLVCGMN GALYLSEMEA SGGKSSLNQA 

       190        200        210        220        230        240 
GAKYGTGYCD AQCYTTPWIN GEGNTESVGS CCQEMDIWEA NARATGLTPH PCNTTGLYEC 

       250        260        270        280        290        300 
SGSGCGDSGV CDKAGCGFNP YGLGAKDYYG YGLKVNTNET FTVVTQFLTN DNTTSGQLSE 

       310        320        330        340        350        360 
IRRLYIQNGQ VIQNAAVTSG GKTVDSITKD FCSGEGSAFN RLGGLEEMGH ALGRGMVLAL 

       370        380        390        400        410 
SIWNDAGSFM QWLDGGSAGP CNATEGNPAL IEKLYPDTHV KFSKIRWGDI GSTYRH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning, purification and characterization of two endo-1,4-beta-glucanases from Aspergillus oryzae KBN616." Kitamoto N., Go M., Shibayama T., Kimura T., Kito Y., Ohmiya K., Tsukagoshi N. Appl. Microbiol. Biotechnol. 46:538-544(1996) [PubMed: 9008887] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES. Strain: KBN616.
[2]	"Genome sequencing and analysis of Aspergillus oryzae." Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E. Kikuchi H. Nature 438:1157-1161(2005) [PubMed: 16372010] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 42149 / RIB 40.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D83732 Genomic DNA. Translation: BAA22589.1. AP007175 Genomic DNA. Translation: BAE66197.1.
RefSeq	XP_001827330.1. XM_001827278.1.
3D structure databases
HSSP	HSSP built from PDB template 1EG1 based on UniProtKB P07981.
ProteinModelPortal	Q2TX26.
SMR	Q2TX26. Positions 18-413.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2TX26.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAORAT00004400; CADAORAP00004325; CADAORAG00004400.
GeneID	5999464.
GenomeReviews	Gene locus celB in contig AP007175_GR.
KEGG	aor:AOR_1_514024.
Phylogenomic databases
GeneTree	EFGT00050000001442.
OrthoDB	EOG4XH37H.
Family and domain databases
InterPro	IPR008985. ConA-like_lec_gl. IPR001722. Glyco_hydro_7. [Graphical view]
Gene3D	G3DSA:2.70.100.10. Glyco_hydro_7. 1 hit.
Pfam	PF00840. Glyco_hydro_7. 1 hit. [Graphical view]
PRINTS	PR00734. GLHYDRLASE7.
SUPFAM	SSF49899. ConA_like_lec_gl. 1 hit.
ProtoNet	Search...

Entry information

Entry name

CELB_ASPOR

Accession

Primary (citable) accession number: Q2TX26
Secondary accession number(s): O13455

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 15, 2010
Last sequence update:	January 24, 2006
Last modified:	January 25, 2012
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents