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B0XWL3

- CBHC_ASPFC

UniProt

B0XWL3 - CBHC_ASPFC

Protein

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

Gene

cbhC

Organism
Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 28 (01 Oct 2014)
      Sequence version 1 (08 Apr 2008)
      Previous versions | rss
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    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

    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:AFUB_046510
    OrganismiNeosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
    Taxonomic identifieri451804 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000001699: Unassembled WGS sequence

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    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_0000394050Add
    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

    Structurei

    3D structure databases

    ProteinModelPortaliB0XWL3.
    SMRiB0XWL3. 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 – 454360Thr-rich linkerAdd
    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

    HOGENOMiHOG000178851.
    OrthoDBiEOG72C594.
    PhylomeDBiB0XWL3.

    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.

    B0XWL3-1 [UniParc]FASTAAdd to Basket

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    MKHLASSIAL TLLLPAVQAQ QTVWGQCGGQ GWSGPTSCVA GAACSTLNPY    50
    YAQCIPGATA TSTTLTTTTA ATTTSQTTTK PTTTGPTTSA PTVTASGNPF 100
    SGYQLYANPY YSSEVHTLAM PSLPSSLQPK ASAVAEVPSF VWLDVAAKVP 150
    TMGTYLADIQ AKNKAGANPP IAGIFVVYDL PDRDCAALAS NGEYSIANNG 200
    VANYKAYIDA IRAQLVKYSD VHTILVIEPD SLANLVTNLN VAKCANAQSA 250
    YLECVDYALK QLNLPNVAMY LDAGHAGWLG WPANLGPAAT LFAKVYTDAG 300
    SPAAVRGLAT NVANYNAWSL STCPSYTQGD PNCDEKKYIN AMAPLLKEAG 350
    FDAHFIMDTS RNGVQPTKQN AWGDWCNVIG TGFGVRPSTN TGDPLQDAFV 400
    WIKPGGESDG TSNSTSPRYD AHCGYSDALQ PAPEAGTWFQ AYFEQLLTNA 450
    NPSF 454
    Length:454
    Mass (Da):47,796
    Last modified:April 8, 2008 - v1
    Checksum:i9EFFB0212288A576
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS499596 Genomic DNA. Translation: EDP53472.1.

    Genome annotation databases

    EnsemblFungiiCADAFUBT00004641; CADAFUBP00004560; CADAFUBG00004641.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS499596 Genomic DNA. Translation: EDP53472.1 .

    3D structure databases

    ProteinModelPortali B0XWL3.
    SMRi B0XWL3. Positions 21-55, 92-454.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAFUBT00004641 ; CADAFUBP00004560 ; CADAFUBG00004641 .

    Phylogenomic databases

    HOGENOMi HOG000178851.
    OrthoDBi EOG72C594.
    PhylomeDBi B0XWL3.

    Family and domain databases

    Gene3Di 3.20.20.40. 1 hit.
    InterProi IPR016288. Beta_cellobiohydrolase.
    IPR000254. Cellulose-bd_dom_fun.
    IPR001524. Glyco_hydro_6_CS.
    [Graphical view ]
    Pfami PF00734. CBM_1. 1 hit.
    PF01341. Glyco_hydro_6. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001100. Beta_cellobiohydrolase. 1 hit.
    PRINTSi PR00733. GLHYDRLASE6.
    ProDomi PD001821. CBD_fun. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00236. fCBD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51989. SSF51989. 1 hit.
    SSF57180. SSF57180. 1 hit.
    PROSITEi PS00562. 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 ]
    ProtoNeti Search...

    Publicationsi

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

    Entry informationi

    Entry nameiCBHC_ASPFC
    AccessioniPrimary (citable) accession number: B0XWL3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 18, 2010
    Last sequence update: April 8, 2008
    Last modified: October 1, 2014
    This is version 28 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