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P19355 (GUX1_HYPRU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Exoglucanase 1
EC=3.2.1.91
Alternative name(s):
1,4-beta-cellobiohydrolase
Exocellobiohydrolase
Exoglucanase I
Gene names
Name:cbh1
OrganismHypocrea rufa (Trichoderma viride)
Taxonomic identifier5547 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Hypocreomycetidae › Hypocreales › Hypocreaceae › Hypocrea

Protein attributes

Sequence length514 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.

Sequence similarities

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

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717
Chain18 – 514497Exoglucanase 1
PRO_0000007928

Regions

Domain478 – 51437CBM1
Region18 – 453436Catalytic
Region454 – 47825Linker

Sites

Active site2291Nucleophile By similarity
Active site2341Proton donor By similarity

Amino acid modifications

Glycosylation621N-linked (GlcNAc...) Potential
Glycosylation811N-linked (GlcNAc...) Potential
Glycosylation2871N-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 bond486 ↔ 503 By similarity
Disulfide bond497 ↔ 513 By similarity

Experimental info

Sequence conflict1731S → T in CAA37878. Ref.1
Sequence conflict2561D → E in CAA37878. Ref.1
Sequence conflict4011N → D in CAA37878. Ref.1
Sequence conflict4141C → S in CAA37878. Ref.1
Sequence conflict4491S → P in CAA37878. Ref.1
Sequence conflict4621Missing Ref.1
Sequence conflict4661R → P Ref.1
Sequence conflict4921S → I in CAA37878. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P19355 [UniParc].

Last modified July 19, 2004. Version 2.
Checksum: C5B1FB734C9CDAF5

FASTA51454,002
        10         20         30         40         50         60 
MYQKLALISA FLATARAQSA CTLQAETHPP LTWQKCSSGG TCTQQTGSVV IDANWRWTHA 

        70         80         90        100        110        120 
TNSSTNCYDG NTWSSTLCPD NETCAKNCCL DGAAYASTYG VTTSADSLSI 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 GQEICDGDSC GGTYSGDRYG GTCDPDGCDW NPYRLGNTSF YGPGSSFTLD 

       310        320        330        340        350        360 
TTKKLTVVTQ FETSGAINRY YVQNGVTFQQ PNAELGDYSG NSLDDDYCAA EEAEFGGSSF 

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

       430        440        450        460        470        480 
PAQLESNSPN AKVVYSNIKF GPIGSTGNSS GGNPPGGNPP GTTTTRRPAT STGSSPGPTQ 

       490        500        510 
THYGQCGGIG YSGPTVCASG STCQVLNPYY SQCL

« Hide

References

[1]"Nucleotide sequence of the cellobiohydrolase gene from Trichoderma viride."
Cheng C., Tsukagoshi N., Udaka S.
Nucleic Acids Res. 18:5559-5559(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Watanabe M.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: MC300-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X53931 Genomic DNA. Translation: CAA37878.1.
AB021656 Genomic DNA. Translation: BAA36215.1.
PIRS11439.

3D structure databases

ProteinModelPortalP19355.
SMRP19355. Positions 18-451, 479-514.
ModBaseSearch...

Protein family/group databases

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

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]
SUPFAMSSF57180. CBD_fun. 1 hit.
SSF49899. ConA_like_lec_gl. 1 hit.
PROSITEPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUX1_HYPRU
AccessionPrimary (citable) accession number: P19355
Secondary accession number(s): O93832
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: July 19, 2004
Last modified: April 3, 2013
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

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