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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

Manual assertion based on experiment ini

  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)DescriptionActionsGraphical viewLength
    Active sitei193Proton donor; for cellulase activityBy similarity1
    Active sitei316Nucleophile; for cellulase activityBy similarity1
    Metal bindingi415Calcium 1PROSITE-ProRule annotation1
    Metal bindingi417Calcium 1PROSITE-ProRule annotation1
    Metal bindingi419Calcium 1PROSITE-ProRule annotation1
    Metal bindingi420Calcium 1; via amide nitrogenPROSITE-ProRule annotation1
    Metal bindingi421Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation1
    Metal bindingi426Calcium 1PROSITE-ProRule annotation1
    Metal bindingi451Calcium 2PROSITE-ProRule annotation1
    Metal bindingi451Calcium 3PROSITE-ProRule annotation1
    Metal bindingi452Calcium 2; via amide nitrogenPROSITE-ProRule annotation1
    Metal bindingi453Calcium 3PROSITE-ProRule annotation1
    Metal bindingi455Calcium 3PROSITE-ProRule annotation1
    Metal bindingi457Calcium 2; via carbonyl oxygenPROSITE-ProRule annotation1
    Metal bindingi457Calcium 3; via carbonyl oxygenPROSITE-ProRule annotation1
    Metal bindingi462Calcium 2PROSITE-ProRule annotation1
    Metal bindingi462Calcium 3PROSITE-ProRule annotation1
    Active sitei612Nucleophile; for esterase activity1 Publication1
    Sitei658Transition state stabilizerBy similarity1
    Sitei705Transition state stabilizerBy similarity1
    Sitei791Increases nucleophilicity of active site Ser1 Publication1

    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

    BioCyciMetaCyc:MONOMER-16425.
    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
    Proteomesi
    • UP000002145 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi612S → A: Loss of esterase activity. 8-fold increase in the binding affinity to cellohexaose. 1 Publication1
    Mutagenesisi789D → A or N: Retains significant esterase activity against 4-NPAc and the polymeric substrates. 1 Publication1
    Mutagenesisi791H → A: Loss of esterase activity. 20-fold decrease in the binding affinity to cellohexaose. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 341 PublicationAdd BLAST34
    ChainiPRO_000000785235 – 814Cellulase/esterase CelEAdd BLAST780

    Interactioni

    Protein-protein interaction databases

    STRINGi203119.Cthe_0797.

    Structurei

    Secondary structure

    1814
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi57 – 64Combined sources8
    Beta strandi66 – 70Combined sources5
    Beta strandi76 – 78Combined sources3
    Turni79 – 82Combined sources4
    Helixi89 – 97Combined sources9
    Beta strandi102 – 105Combined sources4
    Helixi110 – 112Combined sources3
    Turni116 – 118Combined sources3
    Helixi123 – 138Combined sources16
    Beta strandi142 – 145Combined sources4
    Turni151 – 153Combined sources3
    Turni158 – 160Combined sources3
    Helixi161 – 178Combined sources18
    Turni179 – 181Combined sources3
    Beta strandi186 – 190Combined sources5
    Turni200 – 205Combined sources6
    Helixi208 – 226Combined sources19
    Turni230 – 234Combined sources5
    Beta strandi237 – 239Combined sources3
    Helixi242 – 244Combined sources3
    Helixi248 – 251Combined sources4
    Helixi257 – 259Combined sources3
    Beta strandi263 – 268Combined sources6
    Helixi273 – 276Combined sources4
    Helixi288 – 304Combined sources17
    Helixi306 – 308Combined sources3
    Beta strandi312 – 317Combined sources6
    Helixi325 – 340Combined sources16
    Turni341 – 343Combined sources3
    Beta strandi345 – 350Combined sources6
    Turni367 – 370Combined sources4
    Beta strandi371 – 373Combined sources3
    Helixi375 – 385Combined sources11
    Beta strandi493 – 496Combined sources4
    Beta strandi514 – 522Combined sources9
    Beta strandi524 – 540Combined sources17
    Beta strandi548 – 560Combined sources13
    Beta strandi565 – 574Combined sources10
    Helixi578 – 580Combined sources3
    Beta strandi583 – 589Combined sources7
    Beta strandi593 – 595Combined sources3
    Beta strandi603 – 611Combined sources9
    Helixi612 – 615Combined sources4
    Turni616 – 620Combined sources5
    Helixi630 – 632Combined sources3
    Helixi635 – 637Combined sources3
    Helixi639 – 646Combined sources8
    Beta strandi649 – 655Combined sources7
    Helixi665 – 667Combined sources3
    Helixi673 – 676Combined sources4
    Beta strandi679 – 681Combined sources3
    Turni682 – 685Combined sources4
    Helixi690 – 692Combined sources3
    Beta strandi696 – 701Combined sources6
    Helixi704 – 707Combined sources4
    Beta strandi708 – 710Combined sources3
    Helixi714 – 731Combined sources18
    Beta strandi736 – 741Combined sources6
    Helixi747 – 766Combined sources20
    Beta strandi771 – 776Combined sources6
    Helixi788 – 790Combined sources3
    Helixi794 – 812Combined sources19

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2WABX-ray1.90A485-814[»]
    2WAOX-ray1.80A485-814[»]
    4IM4X-ray2.42A/B/C/D/E/F51-386[»]
    ProteinModelPortaliP10477.
    SMRiP10477.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10477.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini409 – 479DockerinPROSITE-ProRule annotationAdd BLAST71

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni35 – 354CellulaseCuratedAdd BLAST320
    Regioni490 – 814EsteraseCuratedAdd BLAST325

    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.
    KOiK01179.
    OMAiCAYGNEG.
    OrthoDBiPOG091H14IK.

    Family and domain databases

    Gene3Di1.10.1330.10. 1 hit.
    3.20.20.80. 1 hit.
    3.40.50.1110. 1 hit.
    InterProiIPR002105. Dockerin_1_rpt.
    IPR016134. Dockerin_dom.
    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)DescriptionActionsGraphical viewLength
    Sequence conflicti147V → L in AAA23224 (PubMed:3066698).Curated1

    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2WABX-ray1.90A485-814[»]
    2WAOX-ray1.80A485-814[»]
    4IM4X-ray2.42A/B/C/D/E/F51-386[»]
    ProteinModelPortaliP10477.
    SMRiP10477.
    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.
    KOiK01179.
    OMAiCAYGNEG.
    OrthoDBiPOG091H14IK.

    Enzyme and pathway databases

    UniPathwayiUPA00114.
    UPA00696.
    BioCyciMetaCyc:MONOMER-16425.

    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.
    InterProiIPR002105. Dockerin_1_rpt.
    IPR016134. Dockerin_dom.
    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...

    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: November 2, 2016
    This is version 102 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.