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Protein

1,4-beta-D-glucan cellobiohydrolase B

Gene

cbhB

Organism
Aspergillus niger
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

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 sitei233 – 2331NucleophileBy similarity
Active sitei238 – 2381Proton 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

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
GH7. Glycoside Hydrolase Family 7.
mycoCLAPiCBH7B_ASPNG.

Names & Taxonomyi

Protein namesi
Recommended name:
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
OrganismiAspergillus niger
Taxonomic identifieri5061 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

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 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 5365151,4-beta-D-glucan cellobiohydrolase BPRO_5000056395Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi351 – 3511N-linked (GlcNAc...)Sequence Analysis
Glycosylationi414 – 4141N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi508 ↔ 525By similarity
Disulfide bondi519 ↔ 535By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Inductioni

Expression is under the control of the xylanolytic transcriptional activator xlnR.2 Publications

Structurei

3D structure databases

ProteinModelPortaliQ9UVS8.
SMRiQ9UVS8. Positions 22-461, 502-536.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini500 – 53637CBM1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni22 – 458437CatalyticAdd
BLAST
Regioni459 – 50042Ser/Thr-rich linkerAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG85664.

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.

Q9UVS8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSFQIYRAA LLLSILATAN AQQVGTYTTE THPSLTWQTC TSDGSCTTND
60 70 80 90 100
GEVVIDANWR WVHSTSSATN CYTGNEWDTS ICTDDVTCAA NCALDGATYE
110 120 130 140 150
ATYGVTTSGS ELRLNFVTQG SSKNIGSRLY LMSDDSNYEL FKLLGQEFTF
160 170 180 190 200
DVDVSNLPCG LNGALYFVAM DADGGTSEYS GNKAGAKYGT GYCDSQCPRD
210 220 230 240 250
LKFINGEANC DGWEPSSNNV NTGVGDHGSC CAEMDVWEAN SISNAFTAHP
260 270 280 290 300
CDSVSQTMCD GDSCGGTYSA SGDRYSGTCD PDGCDYNPYR LGNTDFYGPG
310 320 330 340 350
LTVDTNSPFT VVTQFITDDG TSSGTLTEIK RLYVQNGEVI ANGASTYSSV
360 370 380 390 400
NGSSITSAFC ESEKTLFGDE NVFDKHGGLE GMGEAMAKGM VLVLSLWDDY
410 420 430 440 450
AADMLWLDSD YPVNSSASTP GVARGTCSTD SGVPATVEAE SPNAYVTYSN
460 470 480 490 500
IKFGPIGSTY SSGSSSGSGS SSSSSSTTTK ATSTTLKTTS TTSSGSSSTS
510 520 530
AAQAYGQCGG QGWTGPTTCV SGYTCTYENA YYSQCL
Length:536
Mass (Da):56,219
Last modified:April 30, 2000 - v1
Checksum:iEB904612E2FA3A60
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF156269 Genomic DNA. Translation: AAF04492.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF156269 Genomic DNA. Translation: AAF04492.1.

3D structure databases

ProteinModelPortaliQ9UVS8.
SMRiQ9UVS8. Positions 22-461, 502-536.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
GH7. Glycoside Hydrolase Family 7.
mycoCLAPiCBH7B_ASPNG.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiNOG85664.

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. "Two cellobiohydrolase-encoding genes from Aspergillus niger require D-xylose and the xylanolytic transcriptional activator XlnR for their expression."
    Gielkens M.M., Dekkers E., Visser J., de Graaff L.H.
    Appl. Environ. Microbiol. 65:4340-4345(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
    Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.
  2. "Induction, production, repression, and de-repression of exoglucanase synthesis in Aspergillus niger."
    Hanif A., Yasmeen A., Rajoka M.I.
    Bioresour. Technol. 94:311-319(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.

Entry informationi

Entry nameiCBHB_ASPNG
AccessioniPrimary (citable) accession number: Q9UVS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 19, 2010
Last sequence update: April 30, 2000
Last modified: January 6, 2015
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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.