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Protein

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

Gene

cbhC

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (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 sitei184 – 1841PROSITE-ProRule annotation
Active sitei230 – 2301Proton donorPROSITE-ProRule annotation
Active sitei409 – 4091NucleophilePROSITE-ProRule annotation

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 C (EC:3.2.1.91)
Alternative name(s):
Beta-glucancellobiohydrolase C
Exocellobiohydrolase C
Exoglucanase C
Gene namesi
Name:cbhC
ORF Names:AFUA_3G01910
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000002530: Chromosome 3

Subcellular locationi

Secreted By similarity

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 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 454435Probable 1,4-beta-D-glucan cellobiohydrolase CPRO_0000394051Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi27 ↔ 44By similarity
Disulfide bondi38 ↔ 54By similarity
Disulfide bondi185 ↔ 244By similarity
Disulfide bondi376 ↔ 423By similarity
Glycosylationi413 – 4131N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi5085.CADAFUAP00000253.

Structurei

3D structure databases

ProteinModelPortaliQ4WFK4.
SMRiQ4WFK4. Positions 21-55, 92-454.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 5536CBM1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni59 – 9436Thr-rich linkerAdd
BLAST
Regioni95 – 454360CatalyticAdd
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.
InParanoidiQ4WFK4.
KOiK01238.
OMAiGWPANIQ.
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.

Q4WFK4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKHLASSIAL TLLLPAVQAQ QTVWGQCGGQ GWSGPTSCVA GAACSTLNPY
60 70 80 90 100
YAQCIPGATA TSTTLTTTTA ATTTSQTTTK PTTTGPTTSA PTVTASGNPF
110 120 130 140 150
SGYQLYANPY YSSEVHTLAM PSLPSSLQPK ASAVAEVPSF VWLDVAAKVP
160 170 180 190 200
TMGTYLADIQ AKNKAGANPP IAGIFVVYDL PDRDCAALAS NGEYSIANNG
210 220 230 240 250
VANYKAYIDA IRAQLVKYSD VHTILVIEPD SLANLVTNLN VAKCANAQSA
260 270 280 290 300
YLECVDYALK QLNLPNVAMY LDAGHAGWLG WPANLGPAAT LFAKVYTDAG
310 320 330 340 350
SPAAVRGLAT NVANYNAWSL STCPSYTQGD PNCDEKKYIN AMAPLLKEAG
360 370 380 390 400
FDAHFIMDTS RNGVQPTKQN AWGDWCNVIG TGFGVRPSTN TGDPLQDAFV
410 420 430 440 450
WIKPGGESDG TSNSTSPRYD AHCGYSDALQ PAPEAGTWFQ AYFEQLLTNA

NPSF
Length:454
Mass (Da):47,796
Last modified:July 5, 2005 - v1
Checksum:i9EFFB0212288A576
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000010 Genomic DNA. Translation: EAL86473.1.
RefSeqiXP_748511.1. XM_743418.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00000253; CADAFUAP00000253; CADAFUAG00000253.
GeneIDi3505986.
KEGGiafm:AFUA_3G01910.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000010 Genomic DNA. Translation: EAL86473.1.
RefSeqiXP_748511.1. XM_743418.1.

3D structure databases

ProteinModelPortaliQ4WFK4.
SMRiQ4WFK4. Positions 21-55, 92-454.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5085.CADAFUAP00000253.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFUAT00000253; CADAFUAP00000253; CADAFUAG00000253.
GeneIDi3505986.
KEGGiafm:AFUA_3G01910.

Phylogenomic databases

eggNOGiCOG5297.
HOGENOMiHOG000178851.
InParanoidiQ4WFK4.
KOiK01238.
OMAiGWPANIQ.
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. "Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
    Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.
    , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
    Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Entry informationi

Entry nameiCBHC_ASPFU
AccessioniPrimary (citable) accession number: Q4WFK4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: July 5, 2005
Last modified: January 7, 2015
This is version 55 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.