SubmitCancel

Skip Header

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

P82186

- GUN_MYTED

UniProt

P82186 - GUN_MYTED

(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

Gene
N/A
Organism
Mytilus edulis (Blue mussel)
Status
Reviewed - 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 – 241Nucleophile By similarity
Active sitei132 – 1321Proton donor By 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 – 94
Beta strandi14 – 229
Turni28 – 314
Beta strandi35 – 395
Helixi44 – 463
Beta strandi49 – 535
Helixi54 – 574
Beta strandi63 – 653
Turni67 – 704
Beta strandi72 – 8110
Beta strandi94 – 10310
Turni110 – 1123
Beta strandi116 – 1205
Beta strandi128 – 1347
Helixi141 – 1433
Beta strandi146 – 15510
Helixi157 – 1637
Helixi170 – 1734
Helixi177 – 1793

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WC2X-ray1.20A1-181[»]
ProteinModelPortaliP82186.
SMRiP82186. Positions 1-180.

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

NQKCSGNPRR YNGKSCASTT NYHDSHKGAC GCGPASGDAQ FGWNAGSFVA    50
AASQMYFDSG NKGWCGQHCG QCIKLTTTGG YVPGQGGPVR EGLSKTFMIT 100
NLCPNIYPNQ DWCNQGSQYG GHNKYGYELH LDLENGRSQV TGMGWNNPET 150
TWEVVNCDSE HNHDHRTPSN SMYGQCQCAH Q 181
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:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WC2 X-ray 1.20 A 1-181 [» ]
ProteinModelPortali P82186.
SMRi P82186. Positions 1-180.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH45. Glycoside Hydrolase Family 45.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P82186.

Family and domain databases

InterProi IPR009009. RlpA-like_DPBB.
[Graphical view ]
SUPFAMi SSF50685. SSF50685. 1 hit.
ProtoNeti Search...

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: February 19, 2014
This is version 63 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