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Protein

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

Gene

cbhC

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
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 sitei189 – 1891PROSITE-ProRule annotation
Active sitei235 – 2351Proton donorPROSITE-ProRule annotation
Active sitei414 – 4141NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

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.
GH6. Glycoside Hydrolase Family 6.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable 1,4-beta-D-glucan cellobiohydrolase C (EC:3.2.1.91)
Alternative name(s):
Beta-glucancellobiohydrolase C
Exocellobiohydrolase C
Exoglucanase C
Gene namesi
Name:cbhC
ORF Names:An12g02220
OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
Taxonomic identifieri425011 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006706 Componenti: Chromosome 3L

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 459441Probable 1,4-beta-D-glucan cellobiohydrolase CPRO_5000220698Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 43By similarity
Disulfide bondi37 ↔ 53By similarity
Disulfide bondi190 ↔ 249By similarity
Glycosylationi303 – 3031N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi381 ↔ 428By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi5061.CADANGAP00009490.

Structurei

3D structure databases

ProteinModelPortaliA2QYR9.
SMRiA2QYR9. Positions 20-54, 94-459.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 5436CBM1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni54 – 9441Thr-rich linkerAdd
BLAST
Regioni95 – 459365CatalyticAdd
BLAST

Domaini

Has a modular structure: a carbohydrate-binding module (CBM) at the N-terminus, a linker rich in threonines, and a C-terminal exocellobiohydrolase catalytic module. The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5297.
HOGENOMiHOG000178851.
OrthoDBiEOG72C594.

Family and domain databases

Gene3Di3.20.20.40. 1 hit.
InterProiIPR016288. Beta_cellobiohydrolase.
IPR000254. Cellulose-bd_dom_fun.
IPR001524. Glyco_hydro_6_CS.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view]
PIRSFiPIRSF001100. Beta_cellobiohydrolase. 1 hit.
PRINTSiPR00733. GLHYDRLASE6.
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF51989. SSF51989. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

A2QYR9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHYPLSLALA FLPFGIQAQQ TLWGQCGGQG YSGATSCVAG ATCATVNEYY
60 70 80 90 100
AQCTPAAGTS SATTLKTTTS STTAAVTTTT TTQSPTGSAS PTTTASASGN
110 120 130 140 150
PFSGYQLYVN PYYSSEVASL AIPSLTGSLS SLQAAATAAA KVPSFVWLDT
160 170 180 190 200
AAKVPTMGDY LADIQSQNAA GANPPIAGQF VVYDLPDRDC AALASNGEYS
210 220 230 240 250
IADNGVEHYK SYIDSIREIL VQYSDVHTLL VIEPDSLANL VTNLNVAKCA
260 270 280 290 300
NAESAYLECT NYALTQLNLP NVAMYLDAGH AGWLGWPANQ QPAADLFASV
310 320 330 340 350
YKNASSPAAV RGLATNVANY NAWTISSCPS YTQGNSVCDE QQYINAIAPL
360 370 380 390 400
LQAQGFDAHF IVDTGRNGKQ PTGQQAWGDW CNVINTGFGE RPTTDTGDAL
410 420 430 440 450
VDAFVWVKPG GESDGTSDSS ATRYDAHCGY SDALQPAPEA GTWFQAYFVQ

LLTNANPAF
Length:459
Mass (Da):48,126
Last modified:March 6, 2007 - v1
Checksum:iA584E983E58DCE87
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM270264 Genomic DNA. Translation: CAK41068.1.
RefSeqiXP_001395308.1. XM_001395271.2.

Genome annotation databases

EnsemblFungiiCADANGAT00009671; CADANGAP00009490; CADANGAG00009671.
GeneIDi4985573.
KEGGiang:ANI_1_300104.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM270264 Genomic DNA. Translation: CAK41068.1.
RefSeqiXP_001395308.1. XM_001395271.2.

3D structure databases

ProteinModelPortaliA2QYR9.
SMRiA2QYR9. Positions 20-54, 94-459.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5061.CADANGAP00009490.

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
GH6. Glycoside Hydrolase Family 6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANGAT00009671; CADANGAP00009490; CADANGAG00009671.
GeneIDi4985573.
KEGGiang:ANI_1_300104.

Phylogenomic databases

eggNOGiCOG5297.
HOGENOMiHOG000178851.
OrthoDBiEOG72C594.

Family and domain databases

Gene3Di3.20.20.40. 1 hit.
InterProiIPR016288. Beta_cellobiohydrolase.
IPR000254. Cellulose-bd_dom_fun.
IPR001524. Glyco_hydro_6_CS.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view]
PIRSFiPIRSF001100. Beta_cellobiohydrolase. 1 hit.
PRINTSiPR00733. GLHYDRLASE6.
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF51989. SSF51989. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88."
    Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.
    , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.
    Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CBS 513.88 / FGSC A1513.

Entry informationi

Entry nameiCBHC_ASPNC
AccessioniPrimary (citable) accession number: A2QYR9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: March 6, 2007
Last modified: January 7, 2015
This is version 40 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, Reference 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.