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Q12622 (GUN1_HUMGT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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 EG-1

EC=3.2.1.4
Alternative name(s):
Cellulase
Endo-1,4-beta-glucanase
Gene names
Name:EG-1
OrganismHumicola grisea var. thermoidea
Taxonomic identifier5528 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeHumicola

Protein attributes

Sequence length435 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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.

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
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
Pyrrolidone carboxylic acid
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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 By similarity
Chain21 – 435415Endoglucanase EG-1
PRO_0000007916

Sites

Active site2171Nucleophile By similarity
Active site2221Proton donor By similarity

Amino acid modifications

Modified residue211Pyrrolidone carboxylic acid By similarity
Glycosylation1091N-linked (GlcNAc...) By similarity
Glycosylation2671N-linked (GlcNAc...) By similarity
Disulfide bond38 ↔ 44 By similarity
Disulfide bond71 ↔ 93 By similarity
Disulfide bond83 ↔ 89 By similarity
Disulfide bond160 ↔ 385 By similarity
Disulfide bond192 ↔ 215 By similarity
Disulfide bond196 ↔ 214 By similarity
Disulfide bond235 ↔ 254 By similarity
Disulfide bond243 ↔ 248 By similarity
Disulfide bond259 ↔ 335 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q12622 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 25EB3D62D96B65FA

FASTA43547,890
        10         20         30         40         50         60 
MARGTALLGL TSLLLGLVNG QKPGETKEVH PQLTTFRCTK KGGCKPATNY IVLDSLSHPI 

        70         80         90        100        110        120 
HRAEGLGWGN CGDWGNPPPK DVCPDVESCA KNCIMEGIPD YSQYGVTTNG TSLRLQHILP 

       130        140        150        160        170        180 
DGRVPSPRVY LLDKTERRYE MLHLTGFEFT FDVDATKLPC GMNSALYLSE MHPTGAKSKH 

       190        200        210        220        230        240 
NPGGAYYGTG YCDAQCFVTP FINGLGNIEG KGSCCNEMDI WEANSRASHV APHVCNKKGL 

       250        260        270        280        290        300 
YLCEGEECAF EGVCDKNGCG WNPYRVNVTD YYGRGEEFKV NTLKPFTVVT QFLANRKGKL 

       310        320        330        340        350        360 
EKIHRFYVQD GKIIESFYTN KEGIPYTNMI EDEFCAATGS RKYMELGATQ GMGEALTRGM 

       370        380        390        400        410        420 
VLAMSIWWDQ GGNMEWLDHG EAGPCAKGEG APSNVVQVEP FPEVTYTNLR WGEIGSTYQE 

       430 
VQKPKPKPGP GPRSD 

« Hide

References

[1]Takashima S., Nakamura A., Hidaka M., Masaki H., Uozumi T.
Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: IFO 9854.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D63516 Genomic DNA. Translation: BAA09786.1.

3D structure databases

ProteinModelPortalQ12622.
SMRQ12622. Positions 21-418.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH7. Glycoside Hydrolase Family 7.
mycoCLAPEGL7A_HUMGT.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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. SSF49899. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGUN1_HUMGT
AccessionPrimary (citable) accession number: Q12622
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: February 19, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries