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Q9P8P3 (GUX1_TRIHA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Exoglucanase 1

EC=3.2.1.91
Alternative name(s):
1,4-beta-cellobiohydrolase
Exocellobiohydrolase I
Short name=CBHI
Exoglucanase I
Gene names
Name:cbh1
OrganismTrichoderma harzianum (Hypocrea lixii)
Taxonomic identifier5544 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

Protein attributes

Sequence length505 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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

Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.

Subcellular location

Secreted.

Sequence similarities

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

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

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   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_functioncellulose 1,4-beta-cellobiosidase 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 – 1717 Potential
Chain18 – 505488Exoglucanase 1
PRO_0000007925

Regions

Domain469 – 50537CBM1
Region18 – 449432Catalytic
Region450 – 46920Linker

Sites

Active site1391 By similarity
Active site2251Nucleophile By similarity
Active site2301Proton donor By similarity

Amino acid modifications

Modified residue181Pyrrolidone carboxylic acid By similarity
Glycosylation931N-linked (GlcNAc...) Potential
Glycosylation1261N-linked (GlcNAc...) Potential
Glycosylation2831N-linked (GlcNAc...) Potential
Glycosylation3971N-linked (GlcNAc...) Potential
Disulfide bond21 ↔ 88 By similarity
Disulfide bond36 ↔ 41 By similarity
Disulfide bond66 ↔ 87 By similarity
Disulfide bond77 ↔ 83 By similarity
Disulfide bond151 ↔ 410 By similarity
Disulfide bond185 ↔ 223 By similarity
Disulfide bond189 ↔ 222 By similarity
Disulfide bond243 ↔ 269 By similarity
Disulfide bond251 ↔ 256 By similarity
Disulfide bond274 ↔ 344 By similarity
Disulfide bond477 ↔ 494 By similarity
Disulfide bond488 ↔ 504 By similarity

Secondary structure

................................................................................... 505
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9P8P3 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 52930722F97D7BF0

FASTA50553,216
        10         20         30         40         50         60 
MYRKLAVISA FLAAARAQQV CTQQAETHPP LTWQKCTASG CTPQQGSVVL DANWRWTHDT 

        70         80         90        100        110        120 
KSTTNCYDGN TWSSTLCPDD ATCAKNCCLD GANYSGTYGV TTSGDALTLQ FVTASNVGSR 

       130        140        150        160        170        180 
LYLMANDSTY QEFTLSGNEF SFDVDVSQLP CGLNGALYFV SMDADGGQSK YPGNAAGAKY 

       190        200        210        220        230        240 
GTGYCDSQCP RDLKFINGQA NVEGWEPSSN NANTGVGGHG SCCSEMDIWE ANSISEALTP 

       250        260        270        280        290        300 
HPCETVGQTM CSGDSCGGTY SNDRYGGTCD PDGCDWNPYR LGNTSFYGPG SSFALDTTKK 

       310        320        330        340        350        360 
LTVVTQFATD GSISRYYVQN GVKFQQPNAQ VGSYSGNTIN TDYCAAEQTA FGGTSFTDKG 

       370        380        390        400        410        420 
GLAQINKAFQ GGMVLVMSLW DDYAVNMLWL DSTYPTNATA STPGAKRGSC STSSGVPAQV 

       430        440        450        460        470        480 
EAQSPNSKVI YSNIRFGPIG STGGNTGSNP PGTSTTRAPP SSTGSSPTAT QTHYGQCGGT 

       490        500 
GWTGPTRCAS GYTCQVLNPF YSQCL 

« Hide

References

[1]"Cloning and sequencing of a cellobiohydrolase gene from Trichoderma harzianum FP 108."
Guilfoile P.G., Burns R., Gu Z.-Y., Amundson M., Chang F.-H.
J. Minn. Acad. Sci. 64:18-22(1999)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: FP 108.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF223252 Genomic DNA. Translation: AAF36391.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y9NX-ray2.89A19-449[»]
2YOKX-ray1.67A19-449[»]
ProteinModelPortalQ9P8P3.
SMRQ9P8P3. Positions 18-447, 470-505.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM1. Carbohydrate-Binding Module Family 1.
GH7. Glycoside Hydrolase Family 7.

Proteomic databases

PRIDEQ9P8P3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.70.100.10. 1 hit.
InterProIPR000254. Cellulose-bd_dom_fun.
IPR008985. ConA-like_lec_gl_sf.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamPF00734. CBM_1. 1 hit.
PF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSPR00734. GLHYDRLASE7.
ProDomPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUX1_TRIHA
AccessionPrimary (citable) accession number: Q9P8P3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: October 1, 2000
Last modified: October 16, 2013
This is version 61 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries