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P56680 (GUN1_HUMIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endoglucanase 1
EC=3.2.1.4
Alternative name(s):
Cellulase 1
Endo-1,4-beta-glucanase 1
Endoglucanase I
Gene names
Name:CEL7B
OrganismHumicola insolens (Soft-rot fungus)
Taxonomic identifier34413 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › mitosporic Ascomycota › Humicola

Protein attributes

Sequence length402 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.

Catalytic activity

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

Subunit structure

Monomer.

Subcellular location

Secreted.

Sequence similarities

Belongs to the glycosyl hydrolase 7 (cellulase C) family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentSecreted
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
Pyrrolidone carboxylic acid
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncellulase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 402402Endoglucanase 1
PRO_0000184057

Sites

Active site1971Nucleophile
Active site2021Proton donor

Amino acid modifications

Modified residue11Pyrrolidone carboxylic acid
Glycosylation891N-linked (GlcNAc...)
Glycosylation2471N-linked (GlcNAc...)
Disulfide bond18 ↔ 24
Disulfide bond51 ↔ 73
Disulfide bond63 ↔ 69
Disulfide bond140 ↔ 365
Disulfide bond172 ↔ 195
Disulfide bond176 ↔ 194
Disulfide bond215 ↔ 234
Disulfide bond223 ↔ 228
Disulfide bond239 ↔ 315

Secondary structure

1 ................................................................................. 402
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P56680 [UniParc].

Last modified July 15, 1999. Version 1.
Checksum: E0C6D31375D1635F

FASTA40244,577
        10         20         30         40         50         60 
QKPGETKEVH PQLTTFRCTK RGGCKPATNF IVLDSLSHPI HRAEGLGPGG CGDWGNPPPK 

        70         80         90        100        110        120 
DVCPDVESCA KNCIMEGIPD YSQYGVTTNG TSLRLQHILP DGRVPSPRVY LLDKTKRRYE 

       130        140        150        160        170        180 
MLHLTGFEFT FDVDATKLPC GMNSALYLSE MHPTGAKSKY NPGGAYYGTG YCDAQCFVTP 

       190        200        210        220        230        240 
FINGLGNIEG KGSCCNEMDI WEANSRASHV APHTCNKKGL YLCEGEECAF EGVCDKNGCG 

       250        260        270        280        290        300 
WNNYRVNVTD YYGRGEEFKV NTLKPFTVVT QFLANRRGKL EKIHRFYVQD GKVIESFYTN 

       310        320        330        340        350        360 
KEGVPYTNMI DDEFCEATGS RKYMELGATQ GMGEALTRGM VLAMSIWWDQ GGNMEWLDHG 

       370        380        390        400 
EAGPCAKGEG APSNIVQVEP FPEVTYTNLR WGEIGSTYQE LQ

« Hide

References

[1]"Oligosaccharide specificity of a family 7 endoglucanase: insertion of potential sugar-binding subsites."
Davies G.J., Ducros V., Lewis R.J., Borchert T.V., Schuelein M.
J. Biotechnol. 57:91-100(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT TRP-37/TRP-39.
[2]"Crystal structure of the family 7 endoglucanase I (Cel7B) from Humicola insolens at 2.2 A resolution and identification of the catalytic nucleophile by trapping of the covalent glycosyl-enzyme intermediate."
MacKenzie L.F., Sulzenbacher G., Divne C., Jones T.A., Woeldike H.F., Schuelein M., Withers S.G., Davies G.J.
Biochem. J. 335:409-416(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), MUTAGENESIS.
+Additional computationally mapped references.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A39X-ray2.20A2-402[»]
1DYMX-ray1.75A2-402[»]
1OJIX-ray2.15A2-402[»]
1OJJX-ray1.40A/B2-402[»]
1OJKX-ray1.50A/B2-402[»]
2A39X-ray2.20A/B2-398[»]
ProteinModelPortalP56680.
SMRP56680. Positions 1-398.
ModBaseSearch...

Protein family/group databases

Allergome8280. Hum in Cellulase.
CAZyGH7. Glycoside Hydrolase Family 7.
mycoCLAPEGL7B_HUMIN.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-17623.

Family and domain databases

Gene3D2.70.100.10. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamPF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSPR00734. GLHYDRLASE7.
SUPFAMSSF49899. ConA_like_lec_gl. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP56680.

Entry information

Entry nameGUN1_HUMIN
AccessionPrimary (citable) accession number: P56680
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 15, 1999
Last modified: April 3, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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