Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P17877

- GUN1_CLOJO

UniProt

P17877 - GUN1_CLOJO

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Endoglucanase 1

Gene
N/A
Organism
Clostridium josui
Status
Reviewed - 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

  1. cellulase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›25›25Endoglucanase 1PRO_0000184077Add
BLAST

Sequencei

Sequence statusi: Fragment.

P17877 [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)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei25 – 251

Sequence databases

PIRiA45920.

Cross-referencesi

Sequence databases

PIRi A45920.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

ProtoNeti Search...

Publicationsi

  1. "Purification and properties of an endo-1,4-beta-glucanase from Clostridium josui."
    Fujino T., Sukhumavasi J., Sasaki T., Ohmiya K., Shimizu S.
    J. Bacteriol. 171:4076-4079(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.

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

External Data

Dasty 3