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P10477

- GUNE_CLOTM

UniProt

P10477 - GUNE_CLOTM

Protein

Endoglucanase E

Gene

celE

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 91 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    Functioni

    This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei193 – 1931Proton donorBy similarity
    Active sitei316 – 3161NucleophileBy similarity

    GO - Molecular functioni

    1. cellulase activity Source: UniProtKB-EC
    2. hydrolase activity, acting on ester bonds Source: InterPro

    GO - Biological processi

    1. cellulose catabolic process Source: UniProtKB-KW
    2. lipid metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

    Protein family/group databases

    CAZyiGH5. Glycoside Hydrolase Family 5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoglucanase E (EC:3.2.1.4)
    Alternative name(s):
    Cellulase E
    Endo-1,4-beta-glucanase E
    Short name:
    EgE
    Gene namesi
    Name:celE
    OrganismiClostridium thermocellum (Ruminiclostridium thermocellum)
    Taxonomic identifieri1515 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 34341 PublicationAdd
    BLAST
    Chaini35 – 814780Endoglucanase EPRO_0000007852Add
    BLAST

    Structurei

    Secondary structure

    1
    814
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi57 – 648
    Beta strandi66 – 705
    Beta strandi76 – 783
    Turni79 – 824
    Helixi89 – 979
    Beta strandi102 – 1054
    Helixi110 – 1123
    Turni116 – 1183
    Helixi123 – 13816
    Beta strandi142 – 1454
    Turni151 – 1533
    Turni158 – 1603
    Helixi161 – 17818
    Turni179 – 1813
    Beta strandi186 – 1905
    Turni200 – 2056
    Helixi208 – 22619
    Turni230 – 2345
    Beta strandi237 – 2393
    Helixi242 – 2443
    Helixi248 – 2514
    Helixi257 – 2593
    Beta strandi263 – 2686
    Helixi273 – 2764
    Helixi288 – 30417
    Helixi306 – 3083
    Beta strandi312 – 3176
    Helixi325 – 34016
    Turni341 – 3433
    Beta strandi345 – 3506
    Turni367 – 3704
    Beta strandi371 – 3733
    Helixi375 – 38511
    Beta strandi493 – 4964
    Beta strandi514 – 5229
    Beta strandi524 – 54017
    Beta strandi548 – 56013
    Beta strandi565 – 57410
    Helixi578 – 5803
    Beta strandi583 – 5897
    Beta strandi593 – 5953
    Beta strandi603 – 6119
    Helixi612 – 6154
    Turni616 – 6205
    Helixi630 – 6323
    Helixi635 – 6373
    Helixi639 – 6468
    Beta strandi649 – 6557
    Helixi665 – 6673
    Helixi673 – 6764
    Beta strandi679 – 6813
    Turni682 – 6854
    Helixi690 – 6923
    Beta strandi696 – 7016
    Helixi704 – 7074
    Beta strandi708 – 7103
    Helixi714 – 73118
    Beta strandi736 – 7416
    Helixi747 – 76620
    Beta strandi771 – 7766
    Helixi788 – 7903
    Helixi794 – 81219

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WABX-ray1.90A485-814[»]
    2WAOX-ray1.80A485-814[»]
    4IM4X-ray2.42A/B/C/D/E/F51-386[»]
    ProteinModelPortaliP10477.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10477.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati415 – 438241Add
    BLAST
    Repeati451 – 474242Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni415 – 474602 X 24 AA approximate repeatsAdd
    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

    Keywords - Domaini

    Repeat, Signal

    Family and domain databases

    Gene3Di1.10.1330.10. 1 hit.
    3.20.20.80. 1 hit.
    3.40.50.1110. 1 hit.
    InterProiIPR016134. Cellulos_enz_dockerin_1.
    IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
    IPR018242. Dockerin_1.
    IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR001087. Lipase_GDSL.
    IPR013831. SGNH_hydro-type_esterase_dom.
    [Graphical view]
    PfamiPF00150. Cellulase. 1 hit.
    PF00404. Dockerin_1. 2 hits.
    PF00657. Lipase_GDSL. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF63446. SSF63446. 1 hit.
    PROSITEiPS00448. CLOS_CELLULOSOME_RPT. 2 hits.
    PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P10477-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKIVSLVCV LVMLVSILGS FSVVAASPVK GFQVSGTKLL DASGNELVMR    50
    GMRDISAIDL VKEIKIGWNL GNTLDAPTET AWGNPRTTKA MIEKVREMGF 100
    NAVRVPVTWD THIGPAPDYK IDEAWLNRVE EVVNYVLDCG MYAIINLHHD 150
    NTWIIPTYAN EQRSKEKLVK VWEQIATRFK DYDDHLLFET MNEPREVGSP 200
    MEWMGGTYEN RDVINRFNLA VVNTIRASGG NNDKRFILVP TNAATGLDVA 250
    LNDLVIPNND SRVIVSIHAY SPYFFAMDVN GTSYWGSDYD KASLTSELDA 300
    IYNRFVKNGR AVIIGEFGTI DKNNLSSRVA HAEHYAREAV SRGIAVFWWD 350
    NGYYNPGDAE TYALLNRKTL SWYYPEIVQA LMRGAGVEPL VSPTPTPTLM 400
    PTPSPTVTAN ILYGDVNGDG KINSTDCTML KRYILRGIEE FPSPSGIIAA 450
    DVNADLKINS TDLVLMKKYL LRSIDKFPAE DSQTPDEDNP GILYNGRFDF 500
    SDPNGPKCAW SGSNVELNFY GTEASVTIKS GGENWFQAIV DGNPLPPFSV 550
    NATTSTVKLV SGLAEGAHHL VLWKRTEASL GEVQFLGFDF GSGKLLAAPK 600
    PLERKIEFIG DSITCAYGNE GTSKEQSFTP KNENSYMSYA AITARNLNAS 650
    ANMIAWSGIG LTMNYGGAPG PLIMDRYPYT LPYSGVRWDF SKYVPQVVVI 700
    NLGTNDFSTS FADKTKFVTA YKNLISEVRR NYPDAHIFCC VGPMLWGTGL 750
    DLCRSYVTEV VNDCNRSGDL KVYFVEFPQQ DGSTGYGEDW HPSIATHQLM 800
    AERLTAEIKN KLGW 814
    Length:814
    Mass (Da):90,244
    Last modified:July 1, 1989 - v1
    Checksum:iC6FA24B8D1523632
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22759 Genomic DNA. Translation: AAA23224.1.
    PIRiJT0347. CZCLEM.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22759 Genomic DNA. Translation: AAA23224.1 .
    PIRi JT0347. CZCLEM.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2WAB X-ray 1.90 A 485-814 [» ]
    2WAO X-ray 1.80 A 485-814 [» ]
    4IM4 X-ray 2.42 A/B/C/D/E/F 51-386 [» ]
    ProteinModelPortali P10477.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH5. Glycoside Hydrolase Family 5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P10477.

    Family and domain databases

    Gene3Di 1.10.1330.10. 1 hit.
    3.20.20.80. 1 hit.
    3.40.50.1110. 1 hit.
    InterProi IPR016134. Cellulos_enz_dockerin_1.
    IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
    IPR018242. Dockerin_1.
    IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR001087. Lipase_GDSL.
    IPR013831. SGNH_hydro-type_esterase_dom.
    [Graphical view ]
    Pfami PF00150. Cellulase. 1 hit.
    PF00404. Dockerin_1. 2 hits.
    PF00657. Lipase_GDSL. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    SSF63446. SSF63446. 1 hit.
    PROSITEi PS00448. CLOS_CELLULOSOME_RPT. 2 hits.
    PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Conserved reiterated domains in Clostridium thermocellum endoglucanases are not essential for catalytic activity."
      Hall J., Hazlewood G.P., Barker P.J., Gilbert H.J.
      Gene 69:29-38(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 35-58.

    Entry informationi

    Entry nameiGUNE_CLOTM
    AccessioniPrimary (citable) accession number: P10477
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 91 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

    3D-structure, Direct protein sequencing

    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