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Protein

Endoglucanase

Gene
N/A
Organism
Mytilus edulis (Blue mussel)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Active towards the soluble carboxymethylcellulose (CMC). Possesses expansin activity too.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 4.6.

Temperature dependencei

Optimum temperature is 30-50 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei24 – 241NucleophileBy similarity
Active sitei132 – 1321Proton donorBy 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

CAZyiGH45. Glycoside Hydrolase Family 45.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase (EC:3.2.1.4)
Alternative name(s):
CMCase
Cellulase
Endo-1,4-beta-glucanase
OrganismiMytilus edulis (Blue mussel)
Taxonomic identifieri6550 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaBivalviaPteriomorphiaMytiloidaMytiloideaMytilidaeMytilinaeMytilus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 181181EndoglucanasePRO_0000184075Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi4 ↔ 16
Disulfide bondi30 ↔ 69
Disulfide bondi32 ↔ 176
Disulfide bondi65 ↔ 178
Disulfide bondi72 ↔ 157
Disulfide bondi103 ↔ 113

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Digestive gland.

Structurei

Secondary structure

1
181
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni6 – 94Combined sources
Beta strandi14 – 229Combined sources
Turni28 – 314Combined sources
Beta strandi35 – 395Combined sources
Helixi44 – 463Combined sources
Beta strandi49 – 535Combined sources
Helixi54 – 574Combined sources
Beta strandi63 – 653Combined sources
Turni67 – 704Combined sources
Beta strandi72 – 8110Combined sources
Beta strandi94 – 10310Combined sources
Turni110 – 1123Combined sources
Beta strandi116 – 1205Combined sources
Beta strandi128 – 1347Combined sources
Helixi141 – 1433Combined sources
Beta strandi146 – 15510Combined sources
Helixi157 – 1637Combined sources
Helixi170 – 1734Combined sources
Helixi177 – 1793Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WC2X-ray1.20A1-181[»]
ProteinModelPortaliP82186.
SMRiP82186. Positions 1-180.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP82186.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

InterProiIPR009009. RlpA-like_DPBB.
[Graphical view]
SUPFAMiSSF50685. SSF50685. 1 hit.

Sequencei

Sequence statusi: Complete.

P82186-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
NQKCSGNPRR YNGKSCASTT NYHDSHKGAC GCGPASGDAQ FGWNAGSFVA
60 70 80 90 100
AASQMYFDSG NKGWCGQHCG QCIKLTTTGG YVPGQGGPVR EGLSKTFMIT
110 120 130 140 150
NLCPNIYPNQ DWCNQGSQYG GHNKYGYELH LDLENGRSQV TGMGWNNPET
160 170 180
TWEVVNCDSE HNHDHRTPSN SMYGQCQCAH Q
Length:181
Mass (Da):19,711
Last modified:January 11, 2001 - v1
Checksum:iE00A8C57203823F6
GO

Mass spectrometryi

Molecular mass is 19702 Da from positions 1 - 181. Determined by MALDI. 1 Publication

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WC2X-ray1.20A1-181[»]
ProteinModelPortaliP82186.
SMRiP82186. Positions 1-180.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH45. Glycoside Hydrolase Family 45.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP82186.

Family and domain databases

InterProiIPR009009. RlpA-like_DPBB.
[Graphical view]
SUPFAMiSSF50685. SSF50685. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Purification, characterization and amino-acid sequence analysis of a thermostable, low molecular mass endo-beta-1,4-glucanase from blue mussel, Mytilus edulis."
    Xu B., Hellman U., Ersson B., Janson J.-C.
    Eur. J. Biochem. 267:4970-4977(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY.
    Tissue: Digestive gland.

Entry informationi

Entry nameiGUN_MYTED
AccessioniPrimary (citable) accession number: P82186
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 11, 2001
Last modified: November 26, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.