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Q0CMT2 (CBHB_ASPTN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 33. 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:
Probable 1,4-beta-D-glucan cellobiohydrolase B

EC=3.2.1.91
Alternative name(s):
Beta-glucancellobiohydrolase B
Exocellobiohydrolase B
Exoglucanase B
Gene names
Name:cbhB
ORF Names:ATEG_05002
OrganismAspergillus terreus (strain NIH 2624 / FGSC A1156) [Complete proteome]
Taxonomic identifier341663 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length541 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 By similarity.

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 Probable.

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
   Technical termComplete proteome
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 – 2323 Potential
Chain24 – 541518Probable 1,4-beta-D-glucan cellobiohydrolase B
PRO_0000393549

Regions

Domain505 – 54137CBM1
Region24 – 458435Catalytic
Region459 – 50547Ser/Thr-rich linker

Sites

Active site2351Nucleophile By similarity
Active site2401Proton donor By similarity

Amino acid modifications

Glycosylation2931N-linked (GlcNAc...) Potential
Disulfide bond513 ↔ 530 By similarity
Disulfide bond524 ↔ 540 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0CMT2 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: B72B0BA4C5C9C263

FASTA54157,294
        10         20         30         40         50         60 
MPSTYDIYKK LLLLASFLSA SQAQQVGTSK AEVHPSLTWQ TCTSGGSCTT VNGKVVVDAN 

        70         80         90        100        110        120 
WRWVHNVDGY NNCYTGNTWD TTLCPDDETC ASNCALEGAD YSGTYGVTTS GNSLRLNFVT 

       130        140        150        160        170        180 
QASQKNIGSR LYLMEDDSTY KMFKLLNQEF TFDVDVSNLP CGLNGAVYFV SMDADGGMAK 

       190        200        210        220        230        240 
YPANKAGAKY GTGYCDSQCP RDLKFINGMA NVEGWEPSAN DANAGTGNHG SCCAEMDIWE 

       250        260        270        280        290        300 
ANSISTAYTP HPCDTPGQVM CTGDSCGGTY SSDRYGGTCD PDGCDFNSYR QGNKTFYGPG 

       310        320        330        340        350        360 
MTVDTKSKIT VVTQFLTNDG TASGTLSEIK RFYVQNGKVI PNSESTWSGV SGNSITTAYC 

       370        380        390        400        410        420 
NAQKTLFGDT DVFTKHGGME GMGAALAEGM VLVLSLWDDH NSNMLWLDSN YPTDKPSTTP 

       430        440        450        460        470        480 
GVARGSCDIS SGDPKDVEAN DANAYVVYSN IKVGPIGSTF SGSTGGGSSS STTATSKTTT 

       490        500        510        520        530        540 
TSATKTTTTT TKTTTTTSAS STSTGGAQHW AQCGGIGWTG PTTCVAPYTC QKQNDYYSQC 


L 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH476600 Genomic DNA. Translation: EAU34071.1.
RefSeqXP_001214180.1. XM_001214180.1.

3D structure databases

ProteinModelPortalQ0CMT2.
SMRQ0CMT2. Positions 24-461, 507-541.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING33178.CADATEAP00005220.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADATEAT00005220; CADATEAP00005220; CADATEAG00005220.
GeneID4321099.

Phylogenomic databases

HOGENOMHOG000182210.
OMARGSCDIS.
OrthoDBEOG7ZGXCF.

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 nameCBHB_ASPTN
AccessionPrimary (citable) accession number: Q0CMT2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: October 17, 2006
Last modified: May 14, 2014
This is version 33 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