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P10474

- GUNB_CALSA

UniProt

P10474 - GUNB_CALSA

Protein

Endoglucanase/exoglucanase B

Gene

celB

Organism
Caldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    Functioni

    This protein is made up of two domains: the N-terminal domain has exoglucanase activity while the C-terminal domain is an endoglucanase.

    Catalytic activityi

    Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
    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 sitei177 – 1771Proton donorSequence Analysis
    Active sitei285 – 2851NucleophilePROSITE-ProRule annotation
    Active sitei792 – 7921By similarity

    GO - Molecular functioni

    1. cellulase activity Source: UniProtKB-EC
    2. cellulose 1,4-beta-cellobiosidase activity Source: UniProtKB-EC
    3. 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

    CAZyiCBM3. Carbohydrate-Binding Module Family 3.
    GH10. Glycoside Hydrolase Family 10.
    GH5. Glycoside Hydrolase Family 5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoglucanase/exoglucanase B
    Including the following 2 domains:
    Alternative name(s):
    Cellobiohydrolase
    Cellulase
    Endo-1,4-beta-glucanase
    Exoglucanase (EC:3.2.1.91)
    Alternative name(s):
    1,4-beta-cellobiohydrolase
    Exocellobiohydrolase
    Gene namesi
    Name:celB
    OrganismiCaldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum)
    Taxonomic identifieri44001 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2828Add
    BLAST
    Chaini29 – 10391011Endoglucanase/exoglucanase BPRO_0000007983Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP10474.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini418 – 571154CBM3PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi376 – 41641Pro/Thr-richAdd
    BLAST
    Compositional biasi574 – 61845Pro/Thr-richAdd
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the glycosyl hydrolase 10 (cellulase F) family.Curated
    In the C-terminal section; belongs to the glycosyl hydrolase 5 (cellulase A) family.Curated
    Contains 1 CBM3 (carbohydrate binding type-3) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Family and domain databases

    Gene3Di2.60.40.710. 1 hit.
    3.20.20.80. 2 hits.
    InterProiIPR008965. Carb-bd_dom.
    IPR001956. CBD_3.
    IPR001000. Glyco_hydro_10.
    IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00942. CBM_3. 1 hit.
    PF00150. Cellulase. 1 hit.
    PF00331. Glyco_hydro_10. 1 hit.
    [Graphical view]
    PRINTSiPR00134. GLHYDRLASE10.
    SMARTiSM01067. CBM_3. 1 hit.
    SM00633. Glyco_10. 1 hit.
    [Graphical view]
    SUPFAMiSSF49384. SSF49384. 1 hit.
    SSF51445. SSF51445. 2 hits.
    PROSITEiPS51172. CBM3. 1 hit.
    PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
    PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P10474-1 [UniParc]FASTAAdd to Basket

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    MKRNLFRIVS RVVLIAFIAS ISLVGAMSYF PVETQAAPDW SIPSLCESYK     50
    DDFMIGVAIP ARCLSNDTDK RMVLKHFNSI TAENEMKPES LLAGQTSTGL 100
    SYRFSTADAF VDFASTNKIG IRGHTLVWHN QTPDWFFKDS NGQRLSKDAL 150
    LARLKQYIYD VVGRYKGKVY AWDVVNEAID ENQPDSYRRS TWYEICGPEY 200
    IEKAFIWAHE ADPNAKLFYN DYNTEISKKR DFIYNMVKNL KSKGIPIHGI 250
    GMQCHINVNW PSVSEIENSI KLFSSIPGIE IHITELDMSL YNYGSSENYS 300
    TPPQDLLQKQ SQKYKEIFTM LKKYKNVVKS VTFWGLKDDY SWLRSFYGKN 350
    DWPLLFFEDY SAKPAYWAVI EASGVTTSSP TPTPTPTVTV TPTPTPTPTP 400
    TVTATPTPTP TPVSTPATGG QIKVLYANKE TNSTTNTIRP WLKVVNSGSS 450
    SIDLSRVTIR YWYTVDGERA QSAVSDWAQI GASNVTFKFV KLSSSVSGAD 500
    YYLEIGFKSG AGQLQPGKDT GEIQIRFNKS DWSNYNQGND WSWLQSMTSY 550
    GENEKVTAYI DGVLVWGQEP SGATPAPTMT VAPTATPTPT LSPTVTPTPA 600
    PTQTAIPTPT LTPNPTPTSS IPDDTNDDWL YVSGNKIVDK DGRPVWLTGI 650
    NWFGYNTGTN VFDGVWSCNL KDTLAEIANR GFNLLRVPIS AELILNWSQG 700
    IYPKPNINYY VNPELEGKNS LEVFDIVVQT CKEVGLKIML DIHSIKTDAM 750
    GHIYPVWYDE KFTPEDFYKA CEWITNRYKN DDTIIAFDLK NEPHGKPWQD 800
    TTFAKWDNST DINNWKYAAE TCAKRILNIN PNLLIVIEGI EAYPKDDVTW 850
    TSKSSSDYYS TWWGGNLRGV RKYPINLGKY QNKVVYSPHD YGPSVYQQPW 900
    FYPGFTKESL LQDCWRPNWA YIMEENIAPL LIGEWGGHLD GADNEKWMKY 950
    LRDYIIENHI HHTFWCFNAN SGDTGGLVGY DFTTWDEKKY SFLKPALWQD 1000
    SQGRFVGLDH KRPLGTNGKN INITTYYNNN EPEPVPASK 1039
    Length:1,039
    Mass (Da):117,641
    Last modified:July 1, 1989 - v1
    Checksum:i0E0378171594DDAE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13602 Genomic DNA. Translation: CAA31936.1.
    PIRiS02711.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13602 Genomic DNA. Translation: CAA31936.1 .
    PIRi S02711.

    3D structure databases

    ProteinModelPortali P10474.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM3. Carbohydrate-Binding Module Family 3.
    GH10. Glycoside Hydrolase Family 10.
    GH5. Glycoside Hydrolase Family 5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 2.60.40.710. 1 hit.
    3.20.20.80. 2 hits.
    InterProi IPR008965. Carb-bd_dom.
    IPR001956. CBD_3.
    IPR001000. Glyco_hydro_10.
    IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00942. CBM_3. 1 hit.
    PF00150. Cellulase. 1 hit.
    PF00331. Glyco_hydro_10. 1 hit.
    [Graphical view ]
    PRINTSi PR00134. GLHYDRLASE10.
    SMARTi SM01067. CBM_3. 1 hit.
    SM00633. Glyco_10. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49384. SSF49384. 1 hit.
    SSF51445. SSF51445. 2 hits.
    PROSITEi PS51172. CBM3. 1 hit.
    PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
    PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of a gene from Caldocellum saccharolyticum encoding for exocellulase and endocellulase activity."
      Saul D.J., Williams L.C., Love D.R., Chamley L.W., Bergquist P.L.
      Nucleic Acids Res. 17:439-439(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiGUNB_CALSA
    AccessioniPrimary (citable) accession number: P10474
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 97 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Multifunctional enzyme

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3