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Protein

Probable 1,4-beta-D-glucan cellobiohydrolase B

Gene

cbhB

Organism
Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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 activityi

Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei238 – 2381NucleophileBy similarity
Active sitei243 – 2431Proton donorBy similarity

GO - Molecular functioni

  1. cellulose 1,4-beta-cellobiosidase activity Source: UniProtKB-EC
  2. cellulose binding Source: InterPro

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:cbhB
ORF Names:AFUB_077630
OrganismiNeosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Taxonomic identifieri451804 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000001699 Componenti: Unassembled WGS sequence

Subcellular locationi

Secreted Curated

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence AnalysisAdd
BLAST
Chaini27 – 532506Probable 1,4-beta-D-glucan cellobiohydrolase BPRO_0000393547Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi296 – 2961N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi504 ↔ 521By similarity
Disulfide bondi515 ↔ 531By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliB0Y8K2.
SMRiB0Y8K2. Positions 27-463, 500-532.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini496 – 53237CBM1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni27 – 461435CatalyticAdd
BLAST
Regioni462 – 49635Thr-rich linkerAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000182210.
OrthoDBiEOG7ZGXCF.
PhylomeDBiB0Y8K2.

Family and domain databases

Gene3Di2.70.100.10. 1 hit.
InterProiIPR000254. Cellulose-bd_dom_fun.
IPR013320. ConA-like_dom.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSiPR00734. GLHYDRLASE7.
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

B0Y8K2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLASTFSYRM YKTALILAAL LGSGQAQQVG TSQAEVHPSM TWQSCTAGGS
60 70 80 90 100
CTTNNGKVVI DANWRWVHKV GDYTNCYTGN TWDTTICPDD ATCASNCALE
110 120 130 140 150
GANYESTYGV TASGNSLRLN FVTTSQQKNI GSRLYMMKDD STYEMFKLLN
160 170 180 190 200
QEFTFDVDVS NLPCGLNGAL YFVAMDADGG MSKYPTNKAG AKYGTGYCDS
210 220 230 240 250
QCPRDLKFIN GQANVEGWQP SSNDANAGTG NHGSCCAEMD IWEANSISTA
260 270 280 290 300
FTPHPCDTPG QVMCTGDACG GTYSSDRYGG TCDPDGCDFN SFRQGNKTFY
310 320 330 340 350
GPGMTVDTKS KFTVVTQFIT DDGTSSGTLK EIKRFYVQNG KVIPNSESTW
360 370 380 390 400
TGVSGNSITT EYCTAQKSLF QDQNVFEKHG GLEGMGAALA QGMVLVMSLW
410 420 430 440 450
DDHSANMLWL DSNYPTTASS TTPGVARGTC DISSGVPADV EANHPDAYVV
460 470 480 490 500
YSNIKVGPIG STFNSGGSNP GGGTTTTTTT QPTTTTTTAG NPGGTGVAQH
510 520 530
YGQCGGIGWT GPTTCASPYT CQKLNDYYSQ CL
Length:532
Mass (Da):56,457
Last modified:April 8, 2008 - v1
Checksum:i03EBC7D15A5EAE78
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS499599 Genomic DNA. Translation: EDP49733.1.

Genome annotation databases

EnsemblFungiiCADAFUBT00007703; CADAFUBP00007567; CADAFUBG00007703.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS499599 Genomic DNA. Translation: EDP49733.1.

3D structure databases

ProteinModelPortaliB0Y8K2.
SMRiB0Y8K2. Positions 27-463, 500-532.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFUBT00007703; CADAFUBP00007567; CADAFUBG00007703.

Phylogenomic databases

HOGENOMiHOG000182210.
OrthoDBiEOG7ZGXCF.
PhylomeDBiB0Y8K2.

Family and domain databases

Gene3Di2.70.100.10. 1 hit.
InterProiIPR000254. Cellulose-bd_dom_fun.
IPR013320. ConA-like_dom.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSiPR00734. GLHYDRLASE7.
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CEA10 / CBS 144.89 / FGSC A1163.

Entry informationi

Entry nameiCBHB_ASPFC
AccessioniPrimary (citable) accession number: B0Y8K2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: April 8, 2008
Last modified: January 7, 2015
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.