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P06564

- GUN_BACA3

UniProt

P06564 - GUN_BACA3

Protein

Endoglucanase

Gene
N/A
Organism
Bacillus akibai (strain ATCC 43226 / DSM 21942 / JCM 9157 / 1139)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (01 Jan 1988)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

    pH dependencei

    Optimum pH is 9.0.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei190 – 1901Proton donorBy similarity
    Active sitei305 – 3051NucleophileBy similarity

    GO - Molecular functioni

    1. cellulase activity Source: UniProtKB-EC

    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

    CAZyiCBM17. Carbohydrate-Binding Module Family 17.
    CBM28. Carbohydrate-Binding Module Family 28.
    GH5. Glycoside Hydrolase Family 5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoglucanase (EC:3.2.1.4)
    Alternative name(s):
    Alkaline cellulase
    Endo-1,4-beta-glucanase
    OrganismiBacillus akibai (strain ATCC 43226 / DSM 21942 / JCM 9157 / 1139)
    Taxonomic identifieri1236973 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3030Sequence AnalysisAdd
    BLAST
    Chaini31 – 800770EndoglucanasePRO_0000007837Add
    BLAST

    Structurei

    Secondary structure

    1
    800
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi588 – 5903
    Beta strandi594 – 5963
    Beta strandi600 – 6023
    Beta strandi613 – 6175
    Beta strandi620 – 6289
    Turni637 – 6404
    Beta strandi643 – 6475
    Beta strandi658 – 66912
    Beta strandi674 – 6818
    Helixi684 – 6863
    Beta strandi696 – 6994
    Helixi700 – 7056
    Beta strandi712 – 7209
    Beta strandi735 – 74410
    Beta strandi748 – 75912

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UWWX-ray1.40A/B571-761[»]
    ProteinModelPortaliP06564.
    SMRiP06564. Positions 44-570, 578-761.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06564.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.60.120.260. 2 hits.
    3.20.20.80. 1 hit.
    InterProiIPR005086. CBM_fam_17/28.
    IPR008979. Galactose-bd-like.
    IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF03424. CBM_17_28. 2 hits.
    PF00150. Cellulase. 1 hit.
    [Graphical view]
    SUPFAMiSSF49785. SSF49785. 2 hits.
    SSF51445. SSF51445. 1 hit.
    PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P06564-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMLRKKTKQL ISSILILVLL LSLFPTALAA EGNTREDNFK HLLGNDNVKR    50
    PSEAGALQLQ EVDGQMTLVD QHGEKIQLRG MSTHGLQWFP EILNDNAYKA 100
    LANDWESNMI RLAMYVGENG YASNPELIKS RVIKGIDLAI ENDMYVIVDW 150
    HVHAPGDPRD PVYAGAEDFF RDIAALYPNN PHIIYELANE PSSNNNGGAG 200
    IPNNEEGWNA VKEYADPIVE MLRDSGNADD NIIIVGSPNW SQRPDLAADN 250
    PIDDHHTMYT VHFYTGSHAA STESYPPETP NSERGNVMSN TRYALENGVA 300
    VFATEWGTSQ ANGDGGPYFD EADVWIEFLN ENNISWANWS LTNKNEVSGA 350
    FTPFELGKSN ATSLDPGPDQ VWVPEELSLS GEYVRARIKG VNYEPIDRTK 400
    YTKVLWDFND GTKQGFGVNG DSPVEDVVIE NEAGALKLSG LDASNDVSEG 450
    NYWANARLSA DGWGKSVDIL GAEKLTMDVI VDEPTTVSIA AIPQGPSANW 500
    VNPNRAIKVE PTNFVPLEDK FKAELTITSA DSPSLEAIAM HAENNNINNI 550
    ILFVGTEGAD VIYLDNIKVI GTEVEIPVVH DPKGEAVLPS VFEDGTRQGW 600
    DWAGESGVKT ALTIEEANGS NALSWEFGYP EVKPSDNWAT APRLDFWKSD 650
    LVRGENDYVT FDFYLDPVRA TEGAMNINLV FQPPTNGYWV QAPKTYTINF 700
    DELEEPNQVN GLYHYEVKIN VRDITNIQDD TLLRNMMIIF ADVESDFAGR 750
    VFVDNVRFEG AATTEPVEPE PVDPGEETPP VDEKEAKTEQ KEAEKEEKEE 800
    Length:800
    Mass (Da):88,602
    Last modified:January 1, 1988 - v1
    Checksum:i7CCA4D7B6DAD55CF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15743 Genomic DNA. Translation: AAA22305.1.
    D00066 Genomic DNA. Translation: BAA00045.1.
    PIRiA29003.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15743 Genomic DNA. Translation: AAA22305.1 .
    D00066 Genomic DNA. Translation: BAA00045.1 .
    PIRi A29003.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UWW X-ray 1.40 A/B 571-761 [» ]
    ProteinModelPortali P06564.
    SMRi P06564. Positions 44-570, 578-761.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM17. Carbohydrate-Binding Module Family 17.
    CBM28. Carbohydrate-Binding Module Family 28.
    GH5. Glycoside Hydrolase Family 5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P06564.

    Family and domain databases

    Gene3Di 2.60.120.260. 2 hits.
    3.20.20.80. 1 hit.
    InterProi IPR005086. CBM_fam_17/28.
    IPR008979. Galactose-bd-like.
    IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF03424. CBM_17_28. 2 hits.
    PF00150. Cellulase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49785. SSF49785. 2 hits.
    SSF51445. SSF51445. 1 hit.
    PROSITEi PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and nucleotide sequence of the alkaline cellulase gene from the alkalophilic Bacillus sp. strain 1139."
      Fukumori F., Kudo T., Narahashi Y., Horikoshi K.
      J. Gen. Microbiol. 132:2329-2335(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiGUN_BACA3
    AccessioniPrimary (citable) accession number: P06564
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 1, 1988
    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

    Miscellaneous

    Alkalophilic Bacillus sp strain 1139 is not a true cellulolytic micro-organism because the enzyme is unable to hydrolyze native cellulose.

    Keywords - Technical termi

    3D-structure

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3