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Protein

Cellulase/esterase CelE

Gene

celE

Organism
Clostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Ruminiclostridium thermocellum)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Multifunctional enzyme involved in the degradation of plant cell wall polysaccharides. Displays endoglucanase activity against carboxymethyl cellulose (CMC) and barley beta-glucan (PubMed:3066698, PubMed:1991028). Also catalyzes the deacetylation of acetylated birchwood xylan and glucomannan, with a preference for the latter, and of the synthetic substrate 4-nitrophenyl acetate (4-NPAc) (PubMed:19338387).3 Publications

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.2 Publications
Deacetylation of xylans and xylo-oligosaccharides.1 Publication

Enzyme regulationi

Esterase activity of the CE2 module is inhibited when this domain binds to cellohexaose or beta-glucan.1 Publication

Kineticsi

kcat is 7032 min(-1) for the deacetylation of 4-nitrophenyl acetate. kcat is 12 min(-1) for the deacetylation of birchwood xylan. kcat is 1.1 min(-1) for the deacetylation of glucomannan.1 Publication

  1. KM=165 µM for 4-nitrophenyl acetate1 Publication
  2. KM=2.7 mM for acetylated birchwood xylan1 Publication
  3. KM=0.019 mM for acetylated glucomannan1 Publication

    Pathwayi: cellulose degradation

    This protein is involved in the pathway cellulose degradation, which is part of Glycan metabolism.1 Publication
    View all proteins of this organism that are known to be involved in the pathway cellulose degradation and in Glycan metabolism.

    Pathwayi: xylan degradation

    This protein is involved in the pathway xylan degradation, which is part of Glycan degradation.1 Publication
    View all proteins of this organism that are known to be involved in the pathway xylan degradation and in Glycan degradation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei193 – 1931Proton donor; for cellulase activityBy similarity
    Active sitei316 – 3161Nucleophile; for cellulase activityBy similarity
    Metal bindingi415 – 4151Calcium 1PROSITE-ProRule annotation
    Metal bindingi417 – 4171Calcium 1PROSITE-ProRule annotation
    Metal bindingi419 – 4191Calcium 1PROSITE-ProRule annotation
    Metal bindingi420 – 4201Calcium 1; via amide nitrogenPROSITE-ProRule annotation
    Metal bindingi421 – 4211Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation
    Metal bindingi426 – 4261Calcium 1PROSITE-ProRule annotation
    Metal bindingi451 – 4511Calcium 2PROSITE-ProRule annotation
    Metal bindingi451 – 4511Calcium 3PROSITE-ProRule annotation
    Metal bindingi452 – 4521Calcium 2; via amide nitrogenPROSITE-ProRule annotation
    Metal bindingi453 – 4531Calcium 3PROSITE-ProRule annotation
    Metal bindingi455 – 4551Calcium 3PROSITE-ProRule annotation
    Metal bindingi457 – 4571Calcium 2; via carbonyl oxygenPROSITE-ProRule annotation
    Metal bindingi457 – 4571Calcium 3; via carbonyl oxygenPROSITE-ProRule annotation
    Metal bindingi462 – 4621Calcium 2PROSITE-ProRule annotation
    Metal bindingi462 – 4621Calcium 3PROSITE-ProRule annotation
    Active sitei612 – 6121Nucleophile; for esterase activity1 Publication
    Sitei658 – 6581Transition state stabilizerBy similarity
    Sitei705 – 7051Transition state stabilizerBy similarity
    Sitei791 – 7911Increases nucleophilicity of active site Ser1 Publication

    GO - Molecular functioni

    • acetylxylan esterase activity Source: UniProtKB
    • cellulase activity Source: UniProtKB
    • cellulose binding Source: UniProtKB
    • metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    • cellulose catabolic process Source: UniProtKB
    • glucomannan catabolic process Source: UniProtKB
    • xylan catabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00114.
    UPA00696.

    Protein family/group databases

    CAZyiGH5. Glycoside Hydrolase Family 5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cellulase/esterase CelECurated
    Alternative name(s):
    CtCel5C-CE21 Publication
    Including the following 2 domains:
    Cellulase E1 Publication (EC:3.2.1.42 Publications)
    Alternative name(s):
    CtCel5C1 Publication
    Endo-1,4-beta-glucanase E1 Publication
    Short name:
    EGE1 Publication
    Short name:
    Endoglucanase E1 Publication
    Acetylxylan esterase / glucomannan deacetylase1 Publication (EC:3.1.1.-1 Publication, EC:3.1.1.721 Publication)
    Alternative name(s):
    CtCE21 Publication
    Gene namesi
    Name:celE1 Publication
    Ordered Locus Names:Cthe_0797Imported
    OrganismiClostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Ruminiclostridium thermocellum)
    Taxonomic identifieri203119 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium
    ProteomesiUP000002145 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi612 – 6121S → A: Loss of esterase activity. 8-fold increase in the binding affinity to cellohexaose. 1 Publication
    Mutagenesisi789 – 7891D → A or N: Retains significant esterase activity against 4-NPAc and the polymeric substrates. 1 Publication
    Mutagenesisi791 – 7911H → A: Loss of esterase activity. 20-fold decrease in the binding affinity to cellohexaose. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 34341 PublicationAdd
    BLAST
    Chaini35 – 814780Cellulase/esterase CelEPRO_0000007852Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi203119.Cthe_0797.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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
    Domaini409 – 47971DockerinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni35 – 354320CellulaseCuratedAdd
    BLAST
    Regioni490 – 814325EsteraseCuratedAdd
    BLAST

    Domaini

    Contains an N-terminal module that displays cellulase activity (CtCel5C), a central type I dockerin module (Doc) that facilitates the integration of the enzyme into the cellulosome, and a C-terminal module, CtCE2, which displays dual activities: it catalyzes the deacetylation of plant polysaccharides and also potentiates the activity of its appended cellulase catalytic module through its non-catalytic cellulose binding function.2 Publications

    Sequence similaritiesi

    In the N-terminal section; belongs to the glycosyl hydrolase 5 (cellulase A) family.Curated
    In the C-terminal section; belongs to the carbohydrate esterase 2 (CE2) family.1 Publication
    Contains 1 dockerin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiENOG4108K2F. Bacteria.
    COG2730. LUCA.
    OMAiCAYGNEG.

    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.
    IPR013830. SGNH_hydro.
    [Graphical view]
    PfamiPF00150. Cellulase. 1 hit.
    PF00404. Dockerin_1. 2 hits.
    PF13472. Lipase_GDSL_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF52266. SSF52266. 1 hit.
    SSF63446. SSF63446. 1 hit.
    PROSITEiPS00448. CLOS_CELLULOSOME_RPT. 2 hits.
    PS51766. DOCKERIN. 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.

    P10477-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKKIVSLVCV LVMLVSILGS FSVVAASPVK GFQVSGTKLL DASGNELVMR
    60 70 80 90 100
    GMRDISAIDL VKEIKIGWNL GNTLDAPTET AWGNPRTTKA MIEKVREMGF
    110 120 130 140 150
    NAVRVPVTWD THIGPAPDYK IDEAWLNRVE EVVNYVLDCG MYAIINVHHD
    160 170 180 190 200
    NTWIIPTYAN EQRSKEKLVK VWEQIATRFK DYDDHLLFET MNEPREVGSP
    210 220 230 240 250
    MEWMGGTYEN RDVINRFNLA VVNTIRASGG NNDKRFILVP TNAATGLDVA
    260 270 280 290 300
    LNDLVIPNND SRVIVSIHAY SPYFFAMDVN GTSYWGSDYD KASLTSELDA
    310 320 330 340 350
    IYNRFVKNGR AVIIGEFGTI DKNNLSSRVA HAEHYAREAV SRGIAVFWWD
    360 370 380 390 400
    NGYYNPGDAE TYALLNRKTL SWYYPEIVQA LMRGAGVEPL VSPTPTPTLM
    410 420 430 440 450
    PTPSPTVTAN ILYGDVNGDG KINSTDCTML KRYILRGIEE FPSPSGIIAA
    460 470 480 490 500
    DVNADLKINS TDLVLMKKYL LRSIDKFPAE DSQTPDEDNP GILYNGRFDF
    510 520 530 540 550
    SDPNGPKCAW SGSNVELNFY GTEASVTIKS GGENWFQAIV DGNPLPPFSV
    560 570 580 590 600
    NATTSTVKLV SGLAEGAHHL VLWKRTEASL GEVQFLGFDF GSGKLLAAPK
    610 620 630 640 650
    PLERKIEFIG DSITCAYGNE GTSKEQSFTP KNENSYMSYA AITARNLNAS
    660 670 680 690 700
    ANMIAWSGIG LTMNYGGAPG PLIMDRYPYT LPYSGVRWDF SKYVPQVVVI
    710 720 730 740 750
    NLGTNDFSTS FADKTKFVTA YKNLISEVRR NYPDAHIFCC VGPMLWGTGL
    760 770 780 790 800
    DLCRSYVTEV VNDCNRSGDL KVYFVEFPQQ DGSTGYGEDW HPSIATHQLM
    810
    AERLTAEIKN KLGW
    Length:814
    Mass (Da):90,230
    Last modified:October 14, 2015 - v2
    Checksum:i9913A8E252CBBF8D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti147 – 1471V → L in AAA23224 (PubMed:3066698).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M22759 Genomic DNA. Translation: AAA23224.1.
    CP000568 Genomic DNA. Translation: ABN52032.1.
    PIRiJT0347. CZCLEM.
    RefSeqiWP_011837903.1. NC_009012.1.

    Genome annotation databases

    EnsemblBacteriaiABN52032; ABN52032; Cthe_0797.
    KEGGicth:Cthe_0797.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M22759 Genomic DNA. Translation: AAA23224.1.
    CP000568 Genomic DNA. Translation: ABN52032.1.
    PIRiJT0347. CZCLEM.
    RefSeqiWP_011837903.1. NC_009012.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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...

    Protein-protein interaction databases

    STRINGi203119.Cthe_0797.

    Protein family/group databases

    CAZyiGH5. Glycoside Hydrolase Family 5.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiABN52032; ABN52032; Cthe_0797.
    KEGGicth:Cthe_0797.

    Phylogenomic databases

    eggNOGiENOG4108K2F. Bacteria.
    COG2730. LUCA.
    OMAiCAYGNEG.

    Enzyme and pathway databases

    UniPathwayiUPA00114.
    UPA00696.

    Miscellaneous databases

    EvolutionaryTraceiP10477.

    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.
    IPR013830. SGNH_hydro.
    [Graphical view]
    PfamiPF00150. Cellulase. 1 hit.
    PF00404. Dockerin_1. 2 hits.
    PF13472. Lipase_GDSL_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF52266. SSF52266. 1 hit.
    SSF63446. SSF63446. 1 hit.
    PROSITEiPS00448. CLOS_CELLULOSOME_RPT. 2 hits.
    PS51766. DOCKERIN. 1 hit.
    PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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, FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
      Strain: ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372.
    3. "The non-catalytic C-terminal region of endoglucanase E from Clostridium thermocellum contains a cellulose-binding domain."
      Durrant A.J., Hall J., Hazlewood G.P., Gilbert H.J.
      Biochem. J. 273:289-293(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, CELLULOSE-BINDING, DOMAIN.
    4. Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 485-814 OF WILD-TYPE AND MUTANT ALA-612 IN COMPLEX WITH CELLOHEXAOSE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DOMAIN, ENZYME REGULATION, MUTAGENESIS OF SER-612; ASP-789 AND HIS-791, ACTIVE SITE, PATHWAY.
      Strain: ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372.
    5. "Multifunctional cellulase, xylanase, mannanase."
      Bianchetti C.M., Takasuka T.E., Fox B.G.
      Submitted (JAN-2013) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF 51-386.

    Entry informationi

    Entry nameiCELE_CLOTH
    AccessioniPrimary (citable) accession number: P10477
    Secondary accession number(s): A3DDK3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: October 14, 2015
    Last modified: December 9, 2015
    This is version 99 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.