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Q12624 (GUN3_HUMIN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 77. 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 3

EC=3.2.1.4
Alternative name(s):
Cellulase 3
Endo-1,4-beta-glucanase 3
Gene names
Name:CMC3
OrganismHumicola insolens (Soft-rot fungus)
Taxonomic identifier34413 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeHumicola

Protein attributes

Sequence length388 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Biotechnological use

Used as a detergent cellulase. Sold under the name Celluzyme by Novozymes. This special enzyme has three effects: colour brightening, softening and removal of particulate soil. The overall effect is that it helps to preserve the nice appearance of new fabric and restores old fabric so that it looks new again.

Sequence similarities

Belongs to the glycosyl hydrolase 5 (cellulase A) family.

Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: InterPro

   Molecular_functioncellulase activity

Inferred from electronic annotation. Source: UniProtKB-EC

cellulose binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 388372Endoglucanase 3
PRO_0000007863

Regions

Domain17 – 5236CBM1
Region53 – 9139Linker
Region92 – 388297Catalytic

Sites

Active site2151Proton donor By similarity
Active site3221Nucleophile By similarity

Amino acid modifications

Glycosylation921N-linked (GlcNAc...) Potential
Glycosylation1551N-linked (GlcNAc...) Potential
Glycosylation2591N-linked (GlcNAc...) Potential
Disulfide bond24 ↔ 41 By similarity
Disulfide bond35 ↔ 51 By similarity

Experimental info

Sequence conflict81G → S in BAA12676. Ref.2
Sequence conflict3401T → N in BAA12676. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q12624 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: C7CF349DACC10690

FASTA38842,564
        10         20         30         40         50         60 
MKHSVLAGLF ATGALAQGGA WQQCGGVGFS GSTSCVSGYT CVYLNDWYSQ CQPQPTTLRT 

        70         80         90        100        110        120 
TTTPGATSTT RSAPAATSTT PAKGKFKWFG INQSCAEFGK GEYPGLWGKH FTFPSTSSIQ 

       130        140        150        160        170        180 
THINDGFNMF RVAFSMERLA PNQLNAAFDA NYLRNLTETV NFITGKGKYA MLDPHNFGRY 

       190        200        210        220        230        240 
YERIITDKAA FASFFTKLAT HFASNPLVVF DTNNEYHDMD QQLVFDLNQA AIDAIRAAGA 

       250        260        270        280        290        300 
TSQYIMVEGN SWTGAWTWNV TNNNLAALRD PENKLVYQMH QYLDSDGSGT STACVSTQVG 

       310        320        330        340        350        360 
LQRVIGATNW LRQNGKVGLL GEFAGGANSV CQQAIEGMLT HLQENSDVWT GALWWAGGPW 

       370        380 
WGDYIYSFEP PSGIGYTYYN SLLKKYVP 

« Hide

References

[1]"A novel method for efficient expression cloning of fungal enzyme genes."
Dalboege H., Hansen H.P.H.
Mol. Gen. Genet. 243:253-260(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Cloning, sequencing, and expression of a thermostable cellulase gene of Humicola grisea."
Takashima S., Nakamura A., Masaki H., Uozumi T.
Biosci. Biotechnol. Biochem. 61:245-250(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
Strain: IFO 9854.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X76046 Genomic DNA. Translation: CAA53631.1.
D84470 Genomic DNA. Translation: BAA12676.1.
PIRJC5461.
S43920.

3D structure databases

ProteinModelPortalQ12624.
SMRQ12624. Positions 19-52, 86-387.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM1. Carbohydrate-Binding Module Family 1.
GH5. Glycoside Hydrolase Family 5.
mycoCLAPEGL5C_HUMGT.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR000254. Cellulose-bd_dom_fun.
IPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00734. CBM_1. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]
ProDomPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUN3_HUMIN
AccessionPrimary (citable) accession number: Q12624
Secondary accession number(s): Q12620
Entry history
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: November 1, 1996
Last modified: February 19, 2014
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

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries