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Q9UVS8

- CBHB_ASPNG

UniProt

Q9UVS8 - CBHB_ASPNG

Protein

1,4-beta-D-glucan cellobiohydrolase B

Gene

cbhB

Organism
Aspergillus niger
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 58 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      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 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

    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

    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.
    IPR008985. ConA-like_lec_gl_sf.
    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

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    MSSFQIYRAA LLLSILATAN AQQVGTYTTE THPSLTWQTC TSDGSCTTND    50
    GEVVIDANWR WVHSTSSATN CYTGNEWDTS ICTDDVTCAA NCALDGATYE 100
    ATYGVTTSGS ELRLNFVTQG SSKNIGSRLY LMSDDSNYEL FKLLGQEFTF 150
    DVDVSNLPCG LNGALYFVAM DADGGTSEYS GNKAGAKYGT GYCDSQCPRD 200
    LKFINGEANC DGWEPSSNNV NTGVGDHGSC CAEMDVWEAN SISNAFTAHP 250
    CDSVSQTMCD GDSCGGTYSA SGDRYSGTCD PDGCDYNPYR LGNTDFYGPG 300
    LTVDTNSPFT VVTQFITDDG TSSGTLTEIK RLYVQNGEVI ANGASTYSSV 350
    NGSSITSAFC ESEKTLFGDE NVFDKHGGLE GMGEAMAKGM VLVLSLWDDY 400
    AADMLWLDSD YPVNSSASTP GVARGTCSTD SGVPATVEAE SPNAYVTYSN 450
    IKFGPIGSTY SSGSSSGSGS SSSSSSTTTK ATSTTLKTTS TTSSGSSSTS 500
    AAQAYGQCGG QGWTGPTTCV SGYTCTYENA YYSQCL 536
    Length:536
    Mass (Da):56,219
    Last modified:May 1, 2000 - v1
    Checksum:iEB904612E2FA3A60
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF156269 Genomic DNA. Translation: AAF04492.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF156269 Genomic DNA. Translation: AAF04492.1 .

    3D structure databases

    ProteinModelPortali Q9UVS8.
    SMRi Q9UVS8. Positions 22-461, 502-536.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM1. Carbohydrate-Binding Module Family 1.
    GH7. Glycoside Hydrolase Family 7.
    mycoCLAPi CBH7B_ASPNG.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi NOG85664.

    Family and domain databases

    Gene3Di 2.70.100.10. 1 hit.
    InterProi IPR000254. Cellulose-bd_dom_fun.
    IPR008985. ConA-like_lec_gl_sf.
    IPR001722. Glyco_hydro_7.
    [Graphical view ]
    Pfami PF00734. CBM_1. 1 hit.
    PF00840. Glyco_hydro_7. 1 hit.
    [Graphical view ]
    PRINTSi PR00734. GLHYDRLASE7.
    ProDomi PD001821. CBD_fun. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00236. fCBD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 1 hit.
    SSF57180. SSF57180. 1 hit.
    PROSITEi PS00562. CBM1_1. 1 hit.
    PS51164. CBM1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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(1999) [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(2004) [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 20, 2010
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 58 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