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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)DescriptionActionsGraphical viewLength
Active sitei24NucleophileBy similarity1
Active sitei132Proton donorBy similarity1

GO - Molecular functioni

GO - Biological processi

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001840751 – 181EndoglucanaseAdd BLAST181

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi4 ↔ 16
Disulfide bondi30 ↔ 69
Disulfide bondi32 ↔ 176
Disulfide bondi65 ↔ 178
Disulfide bondi72 ↔ 157
Disulfide bondi103 ↔ 113

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP82186.

Expressioni

Tissue specificityi

Digestive gland.

Structurei

Secondary structure

1181
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni6 – 9Combined sources4
Beta strandi14 – 22Combined sources9
Turni28 – 31Combined sources4
Beta strandi35 – 39Combined sources5
Helixi44 – 46Combined sources3
Beta strandi49 – 53Combined sources5
Helixi54 – 57Combined sources4
Beta strandi63 – 65Combined sources3
Turni67 – 70Combined sources4
Beta strandi72 – 81Combined sources10
Beta strandi94 – 103Combined sources10
Turni110 – 112Combined sources3
Beta strandi116 – 120Combined sources5
Beta strandi128 – 134Combined sources7
Helixi141 – 143Combined sources3
Beta strandi146 – 155Combined sources10
Helixi157 – 163Combined sources7
Helixi170 – 173Combined sources4
Helixi177 – 179Combined sources3

3D structure databases

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

Protein family/group databases

CAZyiGH45. Glycoside Hydrolase Family 45.

Proteomic databases

PRIDEiP82186.

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...

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 2, 2016
This is version 69 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

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.