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P62695 (GUX1_TRIKO) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 48. 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:
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 koningii (Hypocrea koningii)
Taxonomic identifier97093 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

Protein attributes

Sequence length513 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

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 By similarity
Chain18 – 513496Exoglucanase 1
PRO_0000007926

Regions

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

Sites

Active site1431 By similarity
Active site2291Nucleophile By similarity
Active site2341Proton donor By similarity

Amino acid modifications

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

Sequences

Sequence LengthMass (Da)Tools
P62695 [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

References

[1]"Molecular cloning and sequence analysis of the cellobiohydrolase I gene from Trichoderma koningii G-39."
Wey T.T., Hseu T.H., Huang L.
Curr. Microbiol. 28:31-39(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: G-39.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X69976 Genomic DNA. Translation: CAA49596.1.

3D structure databases

ProteinModelPortalP62695.
SMRP62695. Positions 18-451, 478-513.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM1. Carbohydrate-Binding Module Family 1.
GH7. Glycoside Hydrolase Family 7.
mycoCLAPCBH7A_TRIKO.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-17641.

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_TRIKO
AccessionPrimary (citable) accession number: P62695
Secondary accession number(s): P00725
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 16, 2013
This is version 48 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