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P07987 (GUX2_HYPJE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Exoglucanase 2

EC=3.2.1.91
Alternative name(s):
1,4-beta-cellobiohydrolase
Exocellobiohydrolase II
Short name=CBHII
Exoglucanase II
Gene names
Name:cbh2
OrganismHypocrea jecorina (Trichoderma reesei)
Taxonomic identifier51453 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

Protein attributes

Sequence length471 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.

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 6 (cellulase B) family.

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-8155616,EBI-8155616

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.3
Chain25 – 471447Exoglucanase 2
PRO_0000007911

Regions

Domain26 – 6237CBM1
Region66 – 10641Linker
Region107 – 471365Catalytic

Sites

Active site1991
Active site2451Proton donor
Active site4251Nucleophile

Amino acid modifications

Glycosylation381N-linked (GlcNAc...) Potential
Glycosylation1111O-linked (Man...) Ref.5
Glycosylation1211O-linked (Man...) Ref.5
Glycosylation1301O-linked (Man...) Ref.5
Glycosylation1331O-linked (Man...) Ref.5
Glycosylation1341O-linked (Man...) Ref.5
Glycosylation1391O-linked (Man...) Ref.5
Glycosylation1461O-linked (Man...) Ref.5
Glycosylation3131N-linked (GlcNAc...) Ref.5
Glycosylation3341N-linked (GlcNAc...) Ref.5
Disulfide bond34 ↔ 51 By similarity
Disulfide bond45 ↔ 61 By similarity
Disulfide bond200 ↔ 259 Ref.5
Disulfide bond392 ↔ 439 Ref.5

Experimental info

Mutagenesis1991D → A: 20% of wild-type activity.
Mutagenesis2451D → A: No measurable activity.
Sequence conflict3591P → R in AAA72922. Ref.2
Sequence conflict4491P → A in AAA72922. Ref.2

Secondary structure

........................................................... 471
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07987 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: C4711BC335B1BD88

FASTA47149,653
        10         20         30         40         50         60 
MIVGILTTLA TLATLAASVP LEERQACSSV WGQCGGQNWS GPTCCASGST CVYSNDYYSQ 

        70         80         90        100        110        120 
CLPGAASSSS STRAASTTSR VSPTTSRSSS ATPPPGSTTT RVPPVGSGTA TYSGNPFVGV 

       130        140        150        160        170        180 
TPWANAYYAS EVSSLAIPSL TGAMATAAAA VAKVPSFMWL DTLDKTPLME QTLADIRTAN 

       190        200        210        220        230        240 
KNGGNYAGQF VVYDLPDRDC AALASNGEYS IADGGVAKYK NYIDTIRQIV VEYSDIRTLL 

       250        260        270        280        290        300 
VIEPDSLANL VTNLGTPKCA NAQSAYLECI NYAVTQLNLP NVAMYLDAGH AGWLGWPANQ 

       310        320        330        340        350        360 
DPAAQLFANV YKNASSPRAL RGLATNVANY NGWNITSPPS YTQGNAVYNE KLYIHAIGPL 

       370        380        390        400        410        420 
LANHGWSNAF FITDQGRSGK QPTGQQQWGD WCNVIGTGFG IRPSANTGDS LLDSFVWVKP 

       430        440        450        460        470 
GGECDGTSDS SAPRFDSHCA LPDALQPAPQ AGAWFQAYFV QLLTNANPSF L 

« Hide

References

[1]"Homologous domains in Trichoderma reesei cellulolytic enzymes: gene sequence and expression of cellobiohydrolase II."
Teeri T.T., Lehtovaara P., Kauppinen S., Salovuori I., Knowles J.
Gene 51:43-52(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: VTT-D-80133.
[2]"Nucleotide sequence and deduced primary structure of cellobiohydrolase II from Trichoderma reesei."
Chen C.M., Gritzali M., Stafford D.W.
Biotechnology (N.Y.) 5:274-278(1987)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 26921 / CBS 392.92 / QM9414.
[3]"The 1,4-beta-glucan cellobiohydrolases of Trichoderma reesei QM 9414."
Faegerstam L.G., Pettersson L.G.
FEBS Lett. 119:97-100(1980)
Cited for: PROTEIN SEQUENCE OF 25-44.
Strain: ATCC 26921 / CBS 392.92 / QM9414.
[4]"Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei."
Rouvinen J., Bergfors T., Teeri T.T., Knowles J.K.C., Jones T.A.
Science 249:380-386(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[5]"The active site of Trichoderma reesei cellobiohydrolase II: the role of tyrosine 169."
Koivula A., Reinikainen T., Ruohonen L., Valkeajaervi A., Claeyssens M., Teleman O., Kleywegt G.J., Szardenings M., Rouvinen J., Jones T.A., Teeri T.T.
Protein Eng. 9:691-699(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), DISULFIDE BONDS, GLYCOSYLATION AT THR-111; THR-121; SER-130; SER-133; SER-134; SER-139; THR-146; ASN-313 AND ASN-334.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M16190 Genomic DNA. Translation: AAA34210.1.
M55080 Genomic DNA. Translation: AAA72922.1.
PIRA26160.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CB2X-ray2.00A/B107-471[»]
1HGWX-ray2.10A/B107-471[»]
1HGYX-ray2.20A/B107-471[»]
1QJWX-ray1.90A/B107-471[»]
1QK0X-ray2.10A/B109-471[»]
1QK2X-ray2.00A/B109-471[»]
3CBHX-ray2.00A107-471[»]
4AU0X-ray1.70A/B109-471[»]
4AX6X-ray2.30A/B109-471[»]
4AX7X-ray1.70A/B/C/D109-471[»]
4I5RX-ray1.50A154-331[»]
A347-471[»]
4I5UX-ray1.22A158-331[»]
A425-471[»]
ProteinModelPortalP07987.
SMRP07987. Positions 29-62, 109-471.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-8401560.
STRING51453.JGI72567.

Protein family/group databases

CAZyCBM1. Carbohydrate-Binding Module Family 1.
GH6. Glycoside Hydrolase Family 6.
mycoCLAPCBH6B_TRIRE.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG5297.
OMAKCANAQS.

Family and domain databases

Gene3D3.20.20.40. 1 hit.
InterProIPR016288. Beta_cellobiohydrolase.
IPR000254. Cellulose-bd_dom_fun.
IPR001524. Glyco_hydro_6_CS.
[Graphical view]
PfamPF00734. CBM_1. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view]
PIRSFPIRSF001100. Beta_cellobiohydrolase. 1 hit.
PRINTSPR00733. GLHYDRLASE6.
ProDomPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMSSF51989. SSF51989. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07987.

Entry information

Entry nameGUX2_HYPJE
AccessionPrimary (citable) accession number: P07987
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: July 9, 2014
This is version 120 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