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)

A1DNL0

- CBHB_NEOFI

UniProt

A1DNL0 - CBHB_NEOFI

Protein

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

Gene

cbhB

Organism
Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 37 (01 Oct 2014)
      Sequence version 1 (23 Jan 2007)
      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.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 sitei238 – 2381NucleophileBy similarity
    Active sitei243 – 2431Proton 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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable 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
    ORF Names:NFIA_057300
    OrganismiNeosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus)
    Taxonomic identifieri331117 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeNeosartorya
    ProteomesiUP000006702: Unassembled WGS sequence

    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 – 2626Sequence AnalysisAdd
    BLAST
    Chaini27 – 530504Probable 1,4-beta-D-glucan cellobiohydrolase BPRO_0000393551Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi296 – 2961N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi502 ↔ 519By similarity
    Disulfide bondi513 ↔ 529By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi36630.CADNFIAP00004294.

    Structurei

    3D structure databases

    ProteinModelPortaliA1DNL0.
    SMRiA1DNL0. Positions 27-463, 496-530.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini494 – 53037CBM1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni27 – 461435CatalyticAdd
    BLAST
    Regioni462 – 49433Ser/Thr-rich linkerAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG85664.
    HOGENOMiHOG000182210.
    OMAiRGSCDIS.
    OrthoDBiEOG7ZGXCF.

    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.

    A1DNL0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLASTFSYRM YKTALILAAL LGSGQAQQVG TSQAEVHPSM TWQSCTAGGS    50
    CTTNNGKVVI DANWRWVHKV GDYTNCYTGN TWDKTLCPDD ATCASNCALE 100
    GANYQSTYGA TTSGDSLRLN FVTTSQQKNI GSRLYMMKDD TTYEMFKLLN 150
    QEFTFDVDVS NLPCGLNGAL YFVAMDADGG MSKYPTNKAG AKYGTGYCDS 200
    QCPRDLKFIN GQANVEGWQP SSNDANAGTG NHGSCCAEMD IWEANSISTA 250
    FTPHPCDTPG QVMCTGDACG GTYSSDRYGG TCDPDGCDFN SFRQGNKTFY 300
    GPGMTVDTKS KFTVVTQFIT DDGTASGTLK EIKRFYVQNG KVIPNSESTW 350
    SGVGGNSITN DYCTAQKSLF KDQNVFAKHG GMEGMGAALA QGMVLVMSLW 400
    DDHAANMLWL DSNYPTTASS STPGVARGTC DISSGVPADV EANHPDASVV 450
    YSNIKVGPIG STFNSGGSNP GGGTTTTAKP TTTTTTAGSP GGTGVAQHYG 500
    QCGGNGWQGP TTCASPYTCQ KLNDFYSQCL 530
    Length:530
    Mass (Da):56,046
    Last modified:January 23, 2007 - v1
    Checksum:i0CEA2686BA4F4539
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS027698 Genomic DNA. Translation: EAW16381.1.
    RefSeqiXP_001258278.1. XM_001258277.1.

    Genome annotation databases

    EnsemblFungiiCADNFIAT00004422; CADNFIAP00004294; CADNFIAG00004422.
    GeneIDi4584793.
    KEGGinfi:NFIA_057300.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS027698 Genomic DNA. Translation: EAW16381.1 .
    RefSeqi XP_001258278.1. XM_001258277.1.

    3D structure databases

    ProteinModelPortali A1DNL0.
    SMRi A1DNL0. Positions 27-463, 496-530.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 36630.CADNFIAP00004294.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADNFIAT00004422 ; CADNFIAP00004294 ; CADNFIAG00004422 .
    GeneIDi 4584793.
    KEGGi nfi:NFIA_057300.

    Phylogenomic databases

    eggNOGi NOG85664.
    HOGENOMi HOG000182210.
    OMAi RGSCDIS.
    OrthoDBi EOG7ZGXCF.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181.

    Entry informationi

    Entry nameiCBHB_NEOFI
    AccessioniPrimary (citable) accession number: A1DNL0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 20, 2010
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 37 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