Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O59843

- CBHB_ASPAC

UniProt

O59843 - CBHB_ASPAC

Protein

1,4-beta-D-glucan cellobiohydrolase B

Gene

cbhB

Organism
Aspergillus aculeatus
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.1 Publication

    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 sitei234 – 2341NucleophileBy similarity
    Active sitei239 – 2391Proton 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.
    mycoCLAPiCBH7A_ASPAC.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    1,4-beta-D-glucan cellobiohydrolase B (EC:3.2.1.91)
    Alternative name(s):
    1,4-beta-D-glucan cellobiohydrolase I
    Beta-glucancellobiohydrolase B
    Exocellobiohydrolase B
    Exoglucanase B
    Gene namesi
    Name:cbhB
    Synonyms:cbhI
    OrganismiAspergillus aculeatus
    Taxonomic identifieri5053 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 5405181,4-beta-D-glucan cellobiohydrolase BPRO_0000007918Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi434 – 4341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi458 – 4581N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi513 ↔ 529By similarity
    Disulfide bondi524 ↔ 539By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiO59843.

    Structurei

    3D structure databases

    ProteinModelPortaliO59843.
    SMRiO59843. Positions 23-462, 507-540.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini505 – 54036CBM1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni23 – 459437CatalyticAdd
    BLAST
    Regioni460 – 50546Ser/Thr-rich linkerAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    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.

    O59843-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVDSFSIYKT ALLLSMLATS NAQQVGTYTA ETHPSLTWQT CSGSGSCTTT    50
    SGSVVIDANW RWVHEVGGYT NCYSGNTWDS SICSTDTTCA SECALEGATY 100
    ESTYGVTTSG SSLRLNFVTT ASQKNIGSRL YLLADDSTYE TFKLFNREFT 150
    FDVDVSNLPC GLNGALYFVS MDADGGVSRF PTNKAGAKYG TGYCDSQCPR 200
    DLKFIDGQAN IEGWEPSSTD VNAGTGNHGS CCPEMDIWEA NSISSAFTAH 250
    PCDSVQQTMC TGDTCGGTYS DTTDRYSGTC DPDGCDFNPY RFGNTNFYGP 300
    GKTVDNSKPF TVVTQFITHD GTDTGTLTEI RRLYVQNGVV IGNGPSTYTA 350
    ASGNSITESF CKAEKTLFGD TNVFETHGGL SAMGDALGDG MVLVLSLWDD 400
    HAADMLWLDS DYPTTSCASS PGVARGTCPT TTGNATYVEA NYPNSYVTYS 450
    NIKFGTLNST YSGTSSGGSS SSSTTLTTKA STSTTSSKTT TTTSKTSTTS 500
    SSSTNVAQLY GQCGGQGWTG PTTCASGTCT KQNDYYSQCL 540
    Length:540
    Mass (Da):57,099
    Last modified:August 1, 1998 - v1
    Checksum:i002D7FD28DF194D0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB002821 mRNA. Translation: BAA25183.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB002821 mRNA. Translation: BAA25183.1 .

    3D structure databases

    ProteinModelPortali O59843.
    SMRi O59843. Positions 23-462, 507-540.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM1. Carbohydrate-Binding Module Family 1.
    GH7. Glycoside Hydrolase Family 7.
    mycoCLAPi CBH7A_ASPAC.

    Proteomic databases

    PRIDEi O59843.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "Cloning, nucleotide sequence, and transcriptional analysis of Aspergillus aculeatus No.F-50 cellobiohydrolase I (cbhI) gene."
      Takada G., Kawaguchi T., Sumitani J., Arai M.
      J. Ferment. Bioeng. 85:1-9(1998)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: F-50.
    2. "Overexpression of Aspergillus aculeatus cellobiohydrolase I in Aspergillus oryzae."
      Kanamasa S., Mochizuki M., Takada G., Kawaguchi T., Sumitani J., Araii M.
      J. Biosci. Bioeng. 95:627-629(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiCBHB_ASPAC
    AccessioniPrimary (citable) accession number: O59843
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 76 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