Skip Header

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

O08342

- GUNA_PAEBA

UniProt

O08342 - GUNA_PAEBA

(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 A

Gene

celA

Organism
Paenibacillus barcinonensis
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Endoglucanase with high activity on carboxymethylcellulose (CMC) and lichenan, but not active on Avicel.1 Publication

Catalytic activityi

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

Enzyme regulationi

Strongly inhibited by Hg2+, Ag+ and Fe3+. To a lesser extent, is also inhibited by Pb2+, Mn2+, Sn2+ and Cu2+. By contrast, Ni2+, Zn2+, Co2+, Ba2+ and NH4+ do not affect enzyme activity, while 10 mM Ca2+, and Mg2+ produce a stimulating effect. Is also strongly inhibited by chemicals such as N-bromosuccinimide and dimethyl(2-dihydroxy-5-nitrobenzyl)sulphonium bromide. Is not affected by N-acetylimidazole.1 Publication

pH dependencei

Optimum pH is 4.0. Highly stable at acid pH. Retains 100% of its activity after 90 minutes incubation at pH 4.5 and 45 degrees Celsius, and 95% of the initial activity is found after 15 days incubation at room temperature and pH 4.5.1 Publication

Temperature dependencei

Optimum temperature is 40 degrees Celsius. Shows 98% and 51% of its maximum activity at 45 and 55 degrees Celsius, respectively.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei187 – 1871Proton donorBy similarity
Active sitei328 – 3281NucleophileBy similarity

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

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase A (EC:3.2.1.4)
Alternative name(s):
Cellulase A
Endo-1,4-beta-D-glucanase A
Gene namesi
Name:celA
OrganismiPaenibacillus barcinonensis
Taxonomic identifieri198119 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesPaenibacillaceaePaenibacillus

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Biotechnological usei

Study of the performance of endoglucanase A on paper manufacture from agricultural fibers shows that treatment with the enzyme improves the properties of the pulp and the quality of paper. CelA treatment enhances the physical properties (stretch and tensile index) of paper from wheat straw, while dewatering properties are slightly diminished.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232CuratedAdd
BLAST
Chaini33 – 400368Endoglucanase APRO_0000371421Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliO08342.
SMRiO08342. Positions 40-400.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O08342-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTKTFKKFSI AGLALLFMAT AAFAGWSTKA SAADMRSLTA AQITAEMGAG
60 70 80 90 100
WNLGNQLEAT VNGTPNETSW GNPTITPELI KKVKAAGFKT IRIPVSYLNY
110 120 130 140 150
IGSAPNYTVN ASWLNRIQQV VDYAYNEGLY VVINMHGDGF HSIPGSWLHV
160 170 180 190 200
NSSNQNVIRD KYQKVWQQVA TRFSAYNERL IFESMNEVFD GNYNNPNTSY
210 220 230 240 250
YGNLNAYNQI FVDTVRKTGG NNNARWLLVP GWNTNIDYTV GNYGFVVPTD
260 270 280 290 300
NFRSSAIPSS QKRIMISAHY YSPWDFAGEE NGNITQWGAT ATNPAKRSTW
310 320 330 340 350
GQEDYLDSQF KSMYDKFVTQ GYPVVMGEFG SIDKSSYDSS NNNYRAVYAK
360 370 380 390 400
AVTATAKKYK LVPVYWDNGF NGQHGFALFN RFNNTVTQQN IINAIMQGMQ
Length:400
Mass (Da):44,799
Last modified:July 1, 1997 - v1
Checksum:iE89CB35BBC6F8AE5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y12512 Genomic DNA. Translation: CAA73113.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y12512 Genomic DNA. Translation: CAA73113.1 .

3D structure databases

ProteinModelPortali O08342.
SMRi O08342. Positions 40-400.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00150. Cellulase. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
PROSITEi PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning of a new endoglucanase gene from Bacillus sp. BP-23 and characterisation of the enzyme. Performance in paper manufacture from cereal straw."
    Blanco A., Diaz P., Martinez J., Vidal T., Torres A.L., Pastor F.I.J.
    Appl. Microbiol. Biotechnol. 50:48-54(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOTECHNOLOGY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
    Strain: DSM 15478 / CECT 7022 / BP-23.

Entry informationi

Entry nameiGUNA_PAEBA
AccessioniPrimary (citable) accession number: O08342
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: July 1, 1997
Last modified: October 29, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3