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Reviewed, UniProtKB/Swiss-Prot P62694 (GUX1_TRIRE)

Last modified January 19, 2010. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Exoglucanase 1
    EC=3.2.1.91
Alternative name(s):
    Exoglucanase I
    Exocellobiohydrolase I
      Short name=CBHI
    1,4-beta-cellobiohydrolase
Gene names
Name: cbh1
OrganismTrichoderma reesei (Hypocrea jecorina)
Taxonomic identifier51453 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Hypocreomycetidae › Hypocreales › Hypocreaceae › Hypocrea

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Protein attributes

Sequence length513 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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.

Miscellaneous

T.reesei produces two different exocellobiohydrolases. They are unique in that they can hydrolyze crystalline cellulose in the absence of endoglucanases.

Sequence similarities

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

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

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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: EC

cellulose binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717
Chain18 – 513496Exoglucanase 1
PRO_0000007927

Regions

Domain477 – 51337CBM1
Region18 – 453436Catalytic
Region454 – 47724Linker

Sites

Active site1431 Probable
Active site2291Nucleophile Ref.2
Active site2341Proton donor Ref.2

Amino acid modifications

Modified residue181Pyrrolidone carboxylic acid
Glycosylation621N-linked (GlcNAc...) Potential
Glycosylation811N-linked (GlcNAc...) Potential
Glycosylation2871N-linked (GlcNAc...) Potential
Glycosylation4011N-linked (GlcNAc...) Potential
Disulfide bond21 ↔ 89
Disulfide bond36 ↔ 42
Disulfide bond67 ↔ 88
Disulfide bond78 ↔ 84
Disulfide bond155 ↔ 414
Disulfide bond189 ↔ 227
Disulfide bond193 ↔ 226
Disulfide bond247 ↔ 273
Disulfide bond255 ↔ 260
Disulfide bond278 ↔ 348
Disulfide bond485 ↔ 502
Disulfide bond496 ↔ 512

Secondary structure

1 ...................................................................................... 513
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P62694-1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 9F5C0A8A854F2C12

FASTA51354,073
        10         20         30         40         50         60 
MYRKLAVISA FLATARAQSA CTLQSETHPP LTWQKCSSGG TCTQQTGSVV IDANWRWTHA 

        70         80         90        100        110        120 
TNSSTNCYDG NTWSSTLCPD NETCAKNCCL DGAAYASTYG VTTSGNSLSI GFVTQSAQKN 

       130        140        150        160        170        180 
VGARLYLMAS DTTYQEFTLL GNEFSFDVDV SQLPCGLNGA LYFVSMDADG GVSKYPTNTA 

       190        200        210        220        230        240 
GAKYGTGYCD SQCPRDLKFI NGQANVEGWE PSSNNANTGI GGHGSCCSEM DIWEANSISE 

       250        260        270        280        290        300 
ALTPHPCTTV GQEICEGDGC GGTYSDNRYG GTCDPDGCDW NPYRLGNTSF YGPGSSFTLD 

       310        320        330        340        350        360 
TTKKLTVVTQ FETSGAINRY YVQNGVTFQQ PNAELGSYSG NELNDDYCTA EEAEFGGSSF 

       370        380        390        400        410        420 
SDKGGLTQFK KATSGGMVLV MSLWDDYYAN MLWLDSTYPT NETSSTPGAV RGSCSTSSGV 

       430        440        450        460        470        480 
PAQVESQSPN AKVTFSNIKF GPIGSTGNPS GGNPPGGNRG TTTTRRPATT TGSSPGPTQS 

       490        500        510 
HYGQCGGIGY SGPTVCASGT TCQVLNPYYS QCL

« Hide

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References

[1]"Molecular cloning of exo-cellobiohydrolase I derived from Trichoderma reesei strain L27."
Shoemaker S., Schweickart V., Ladner M., Gelfand D., Kwok S., Myambo K., Innis M.
Biotechnology (N.Y.) 1:691-696(1983)
Cited for: NUCLEOTIDE SEQUENCE.
Strain: L27.
[2]"Identification of a functionally important carboxyl group in cellobiohydrolase I from Trichoderma reesei."
Tomme P., Clayssens M.
FEBS Lett. 243:239-243(1989)
Cited for: ACTIVE SITE.
[3]"The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei."
Divne C., Staahlberg J., Reinikainen T., Ruohonen L., Pettersson G., Knowles J.K.C., Teeri T.T., Jones T.A.
Science 265:524-528(1994) [PubMed: 8036495] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 18-452.
[4]"High-resolution crystal structures reveal how a cellulose chain is bound in the 50 A long tunnel of cellobiohydrolase I from Trichoderma reesei."
Divne C., Staahlberg J., Teeri T.T., Jones T.A.
J. Mol. Biol. 275:309-325(1998) [PubMed: 9466911] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 18-452.
Strain: QM9414 / Rut C-30.
[5]"Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing."
Kraulis P.J., Clore G.M., Nilges M., Jones T.A., Pettersson G., Knowles J., Gronenborn A.M.
Biochemistry 28:7241-7257(1989) [PubMed: 2554967] [Abstract]
Cited for: STRUCTURE BY NMR OF 478-513.
[6]"Three-dimensional structures of three engineered cellulose-binding domains of cellobiohydrolase I from Trichoderma reesei."
Mattinen M.L., Kontteli M., Kerovuo J., Linder M., Annila A., Lindeberg G., Reinikainen T., Drakenberg T.
Protein Sci. 6:294-303(1997) [PubMed: 9041630] [Abstract]
Cited for: STRUCTURE BY NMR OF 478-513.
+Additional computationally mapped references.

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Cross-references

Sequence databases

PIREUTQI. A00902.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AZ6NMR-A478-513[»]
1AZHNMR-A478-513[»]
1AZJNMR-A478-513[»]
1AZKNMR-A478-513[»]
1CBHNMR-A478-513[»]
1CELX-ray1.80A/B19-451[»]
1DY4X-ray1.90A19-451[»]
1EGNX-ray1.60A19-451[»]
1Q2BX-ray1.60A19-451[»]
1Q2EX-ray1.75A/B19-451[»]
2CBHNMR-A478-513[»]
2CELX-ray2.00A/B19-451[»]
2V3IX-ray1.05A19-451[»]
2V3RX-ray1.60A19-451[»]
3CELX-ray2.00A19-451[»]
4CELX-ray2.20A/B19-451[»]
5CELX-ray1.90A19-451[»]
6CELX-ray1.70A19-451[»]
7CELX-ray1.90A19-451[»]
8CELmodel-A18-451[»]
ModBaseSearch...

Protein family/group databases

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

Enzyme and pathway databases

BRENDA3.2.1.91. 280374.

Family and domain databases

InterProIPR000254. Cellulose-bd_dom_fun.
IPR008985. ConA-like_lec_gl.
IPR001722. Glyco_hydro_7.
[Graphical view]
Gene3DG3DSA:2.70.100.10. Glyco_hydro_7. 1 hit.
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]
PROSITEPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameGUX1_TRIRE
AccessionPrimary (citable) accession number: P62694
Secondary accession number(s): P00725
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 19, 2010
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents