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Q84C00

- GUB_CLOTM

UniProt

Q84C00 - GUB_CLOTM

Protein

Beta-glucanase

Gene

licB

Organism
Clostridium thermocellum (Ruminiclostridium thermocellum)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 55 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei136 – 1361NucleophilePROSITE-ProRule annotation
    Active sitei140 – 1401Proton donorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. licheninase activity Source: UniProtKB-EC

    GO - Biological processi

    1. polysaccharide catabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Protein family/group databases

    CAZyiGH16. Glycoside Hydrolase Family 16.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-glucanase (EC:3.2.1.73)
    Alternative name(s):
    1,3-1,4-beta-D-glucan 4-glucanohydrolase
    Endo-beta-1,3-1,4 glucanase
    Laminarinase
    Lichenase
    Gene namesi
    Name:licB
    Synonyms:lam1
    OrganismiClostridium thermocellum (Ruminiclostridium thermocellum)
    Taxonomic identifieri1515 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Sequence AnalysisAdd
    BLAST
    Chaini28 – 334307Beta-glucanasePRO_0000011792Add
    BLAST

    Interactioni

    Subunit structurei

    May form part of a multienzyme complex (cellulosome).

    Structurei

    3D structure databases

    ProteinModelPortaliQ84C00.
    SMRiQ84C00. Positions 33-246.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati273 – 296241Add
    BLAST
    Repeati308 – 331242Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni273 – 331592 X 24 AA approximate repeatsAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi252 – 26918Pro/Thr-rich (linker)Add
    BLAST

    Domaini

    A 24 residue domain is repeated twice in this enzyme as well as in other C.thermocellum cellulosome enzymes. This domain may function as the binding ligand for the SL component.

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 16 family.Curated

    Keywords - Domaini

    Repeat, Signal

    Family and domain databases

    Gene3Di1.10.1330.10. 1 hit.
    2.60.120.200. 1 hit.
    InterProiIPR008264. Beta_glucanase.
    IPR016134. Cellulos_enz_dockerin_1.
    IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR018242. Dockerin_1.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR000757. Glyco_hydro_16.
    IPR008263. Glycoside_hydrolase_16_AS.
    [Graphical view]
    PfamiPF00404. Dockerin_1. 2 hits.
    PF00722. Glyco_hydro_16. 1 hit.
    [Graphical view]
    PRINTSiPR00737. GLHYDRLASE16.
    SUPFAMiSSF49899. SSF49899. 1 hit.
    SSF63446. SSF63446. 1 hit.
    PROSITEiPS00448. CLOS_CELLULOSOME_RPT. 2 hits.
    PS00018. EF_HAND_1. 2 hits.
    PS01034. GLYCOSYL_HYDROL_F16. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q84C00-1 [UniParc]FASTAAdd to Basket

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    MKNRVISLLM ASLLLVLSVI VAPFYKAEAA TVVNTPFVAV FSNFDSSQWE    50
    KADWANGSVF NCVWKPSQVT FSNGKMILTL DREYGGSYPY KSGEYRSKSF 100
    FGYGYYEVRM KAAKNVGIVS SFFTYTGPSD NNPWDEIDIE FLGKDTTKAQ 150
    FNWYKNEVGG NEYLHNLGFD ASQDFHTYGF EWRPDYIDFY VDGKKVYRGT 200
    RNIPVTPGKI MMNLWPGKGV DEWLGRYDGR TPLQAEYEYV KYYPNGVPQD 250
    NPTPTPTIAP STPTNPNLPL KGDVNGDGHV NSSDYSLFKR YLLRVIDRFP 300
    VGDQSVADVN RDGRIDSTDL TMLKRYLIRA IPSL 334
    Length:334
    Mass (Da):37,942
    Last modified:June 1, 2003 - v1
    Checksum:i3079DEF1CEE5A664
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti97 – 971S → T in CAA41281. (PubMed:1755832)Curated
    Sequence conflicti97 – 971S → T1 PublicationCurated
    Sequence conflicti149 – 1491A → V in CAA41281. (PubMed:1755832)Curated
    Sequence conflicti149 – 1491A → V1 PublicationCurated
    Sequence conflicti157 – 1571E → G in CAA41281. (PubMed:1755832)Curated
    Sequence conflicti157 – 1571E → G1 PublicationCurated
    Sequence conflicti218 – 2181K → I in CAA41281. (PubMed:1755832)Curated
    Sequence conflicti218 – 2181K → I1 PublicationCurated
    Sequence conflicti304 – 33431QSVAD…AIPSL → PQDGCGRHDRVVDSGSK in CAA41281. (PubMed:1755832)CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58392 Genomic DNA. Translation: CAA41281.1.
    AY225318 Genomic DNA. Translation: AAO74890.1.
    PIRiJS0611.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58392 Genomic DNA. Translation: CAA41281.1 .
    AY225318 Genomic DNA. Translation: AAO74890.1 .
    PIRi JS0611.

    3D structure databases

    ProteinModelPortali Q84C00.
    SMRi Q84C00. Positions 33-246.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH16. Glycoside Hydrolase Family 16.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 1.10.1330.10. 1 hit.
    2.60.120.200. 1 hit.
    InterProi IPR008264. Beta_glucanase.
    IPR016134. Cellulos_enz_dockerin_1.
    IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR018242. Dockerin_1.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR000757. Glyco_hydro_16.
    IPR008263. Glycoside_hydrolase_16_AS.
    [Graphical view ]
    Pfami PF00404. Dockerin_1. 2 hits.
    PF00722. Glyco_hydro_16. 1 hit.
    [Graphical view ]
    PRINTSi PR00737. GLHYDRLASE16.
    SUPFAMi SSF49899. SSF49899. 1 hit.
    SSF63446. SSF63446. 1 hit.
    PROSITEi PS00448. CLOS_CELLULOSOME_RPT. 2 hits.
    PS00018. EF_HAND_1. 2 hits.
    PS01034. GLYCOSYL_HYDROL_F16. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the Clostridium thermocellum laminarinase gene."
      Zverlov V.V., Laptev D.A., Tishkov V.I., Velikodvorskaja G.A.
      Biochem. Biophys. Res. Commun. 181:507-512(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: F7.
    2. Zverlov V.V.
      Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. Lv W.-P., Xu Z.-R., Li W.-F., Sun J.-Y., Xu Y.-X., Gu S.-H.
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Cloning the Clostridium thermocellum thermostable laminarinase gene in Escherichia coli; the properties of the enzyme thus produced."
      Zverlov V.V., Velikodvorskaja G.A.
      Biotechnol. Lett. 12:811-816(1990)
      Cited for: CHARACTERIZATION.
      Strain: F7.

    Entry informationi

    Entry nameiGUB_CLOTM
    AccessioniPrimary (citable) accession number: Q84C00
    Secondary accession number(s): P29716, P37074
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 17, 2007
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 55 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic 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