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Protein

Endoglucanase 1

Gene
N/A
Organism
Clostridium josui
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

This enzyme hydrolyzes cellotetraose, cellopentaose, and cellohexaose to cellobiose and cellotriose but does not hydrolyze cellobiose or cellotriose.

Catalytic activityi

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

pH dependencei

Optimum pH is 6.8 with carboxymethyl cellulose (CmC) as substrate.

Temperature dependencei

Optimum temperature is 60 degrees Celsius with carboxymethyl cellulose (CmC) as substrate.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase 1 (EC:3.2.1.4)
Alternative name(s):
Cellulase 1
Endo-1,4-beta-glucanase 1
OrganismiClostridium josui
Taxonomic identifieri1499 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001840771 – ›25Endoglucanase 1Add BLAST›25

Sequencei

Sequence statusi: Fragment.

P17877-1 [UniParc]FASTAAdd to basket

« Hide

        10         20 
YDASLKPNLQ IPQKNIPNND AVNIK
Length:25
Mass (Da):2,808
Last modified:August 1, 1990 - v1
Checksum:iF68D1B4D3BD9DFCB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei251

Sequence databases

PIRiA45920.

Cross-referencesi

Sequence databases

PIRiA45920.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

ProtoNetiSearch...

Entry informationi

Entry nameiGUN1_CLOJO
AccessioniPrimary (citable) accession number: P17877
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: October 1, 2014
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries

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.